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46 results on '"Eric Hampton"'

1. Antitumor activity of a systemic STING-activating non-nucleotide cGAMP mimetic

Author

H. Michael Petrassi, Emily N. Chin, Mildred Kissai, Arnab K. Chatterjee, Dennis W. Wolan, Alan Chu, John R. Teijaro, Ashley K. Woods, Ana M. Gamo, Daniel C. Lazar, Nhan T. Nguyen, Peter G. Schultz, Vincent F. Vartabedian, Ying Jia, Kristen Johnson, Travis S. Young, Manoj Kumar, Sean B. Joseph, Eric Hampton, Francisco Martínez-Peña, Chenguang Yu, William Vernier, Luke L. Lairson, Brent Benish, Sabrina H. Ali, Laura E. Pereira, and Philipp N. Sander

Subjects
Agonist, medicine.drug_class, Protein Conformation, Cell, Guanosine, Antineoplastic Agents, CD8-Positive T-Lymphocytes, Crystallography, X-Ray, B7-H1 Antigen, chemistry.chemical_compound, Mice, Antigen, Biomimetic Materials, medicine, Animals, Humans, Multidisciplinary, Innate immune system, Membrane Proteins, Dendritic Cells, eye diseases, Cell biology, Killer Cells, Natural, Sting, medicine.anatomical_structure, chemistry, Stimulator of interferon genes, Nucleotides, Cyclic, CD8
Abstract

Stimulator of interferon genes (STING) links innate immunity to biological processes ranging from antitumor immunity to microbiome homeostasis. Mechanistic understanding of the anticancer potential for STING receptor activation is currently limited by metabolic instability of the natural cyclic dinucleotide (CDN) ligands. From a pathway-targeted cell-based screen, we identified a non-nucleotide, small-molecule STING agonist, termed SR-717, that demonstrates broad interspecies and interallelic specificity. A 1.8-angstrom cocrystal structure revealed that SR-717 functions as a direct cyclic guanosine monophosphate-adenosine monophosphate (cGAMP) mimetic that induces the same "closed" conformation of STING. SR-717 displayed antitumor activity; promoted the activation of CD8+ T, natural killer, and dendritic cells in relevant tissues; and facilitated antigen cross-priming. SR-717 also induced the expression of clinically relevant targets, including programmed cell death 1 ligand 1 (PD-L1), in a STING-dependent manner.

Published
2020

2. Targeted Delivery of an Anti-inflammatory PDE4 Inhibitor to Immune Cells via an Antibody–drug Conjugate

Author

Aaron D. Pearson, Shan Yu, Reyna Kv Lim, Peter G. Schultz, Sijia Li, Michael J. Bollong, Stephanie A. Kazane, Meredith Weglarz, Travis S. Young, Claudio Zambaldo, Eric Hampton, Timothy M. Wright, Holly Parker, Ashley K. Woods, Jiayin Shen, David T. Rodgers, Danling Wang, and Matthew S. Tremblay

Subjects
Lipopolysaccharides, 0301 basic medicine, Antibody-drug conjugate, Immunoconjugates, medicine.medical_treatment, Inflammation, CD11a, Pharmacology, Monocytes, Mice, 03 medical and health sciences, Therapeutic index, Immune system, Drug Discovery, Genetics, medicine, Animals, Humans, Sulfones, Molecular Biology, Cells, Cultured, biology, CD11 Antigens, Tumor Necrosis Factor-alpha, business.industry, Disease Models, Animal, 030104 developmental biology, Cytokine, Gene Expression Regulation, Aminoquinolines, biology.protein, Molecular Medicine, Original Article, Tumor necrosis factor alpha, Phosphodiesterase 4 Inhibitors, Peritoneum, medicine.symptom, Antibody, business
Abstract

Phosphodiesterase 4 (PDE4) inhibitors are approved for the treatment of some moderate to severe inflammatory conditions. However, dose-limiting side effects in the central nervous system and gastrointestinal tract, including nausea, emesis, headache, and diarrhea, have impeded the broader therapeutic application of PDE4 inhibitors. We sought to exploit the wealth of validation surrounding PDE4 inhibition by improving the therapeutic index through generation of an antibody-drug conjugate (ADC) that selectively targets immune cells through the CD11a antigen. The resulting ADC consisted of a human αCD11a antibody (based on efalizumab clone hu1124) conjugated to an analog of the highly potent PDE4 inhibitor GSK256066. Both the human αCD11a ADC and a mouse surrogate αCD11a ADC (based on the M17 clone) rapidly internalized into immune cells and suppressed lipololysaccharide (LPS)-induced TNFα secretion in primary human monocytes and mouse peritoneal cells, respectively. In a carrageenan-induced air pouch inflammation mouse model, treatment with the ADC significantly reduced inflammatory cytokine production in the air pouch exudate. Overall, these results provide compelling evidence for the feasibility of delivering drugs with anti-inflammatory activity selectively to the immune compartment via CD11a and the development of tissue-targeted PDE4 inhibitors as a promising therapeutic modality for treating inflammatory diseases.

Published
2016
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3. Development of A Chimeric Antigen Receptor Targeting C-Type Lectin-Like Molecule-1 for Human Acute Myeloid Leukemia

Author

Ashley K. Woods, Eduardo Laborda, Chan Hyuk Kim, Peter G. Schultz, Magdalena Mazagova, Xinxin Wang, Sida Shao, David T. Rodgers, Eric Hampton, Herlinda Quirino, and Travis S. Young

Subjects
0301 basic medicine, Cytotoxicity, Immunologic, Myeloid, medicine.medical_treatment, T-Lymphocytes, CD33, Immunotherapy, Adoptive, lcsh:Chemistry, Mice, 0302 clinical medicine, AML, hemic and lymphatic diseases, Medicine, lcsh:QH301-705.5, Spectroscopy, Communication, Myeloid leukemia, General Medicine, Computer Science Applications, Haematopoiesis, Leukemia, Leukemia, Myeloid, Acute, medicine.anatomical_structure, 030220 oncology & carcinogenesis, Female, Stem cell, CLL-1, optimization, Recombinant Fusion Proteins, Receptors, Antigen, T-Cell, Catalysis, Inorganic Chemistry, 03 medical and health sciences, CAR-T-cell, Antigens, Neoplasm, Cell Line, Tumor, Animals, Humans, Lectins, C-Type, Physical and Theoretical Chemistry, Molecular Biology, business.industry, Organic Chemistry, Immunotherapy, medicine.disease, Xenograft Model Antitumor Assays, Chimeric antigen receptor, hematopoiesis, Disease Models, Animal, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, Receptors, Mitogen, Immunology, business, Single-Chain Antibodies
Abstract

The treatment of patients with acute myeloid leukemia (AML) with targeted immunotherapy is challenged by the heterogeneity of the disease and a lack of tumor-exclusive antigens. Conventional immunotherapy targets for AML such as CD33 and CD123 have been proposed as targets for chimeric antigen receptor (CAR)-engineered T-cells (CAR-T-cells), a therapy that has been highly successful in the treatment of B-cell leukemia and lymphoma. However, CD33 and CD123 are present on hematopoietic stem cells, and targeting with CAR-T-cells has the potential to elicit long-term myelosuppression. C-type lectin-like molecule-1 (CLL1 or CLEC12A) is a myeloid lineage antigen that is expressed by malignant cells in more than 90% of AML patients. CLL1 is not expressed by healthy Hematopoietic Stem Cells (HSCs), and is therefore a promising target for CAR-T-cell therapy. Here, we describe the development and optimization of an anti-CLL1 CAR-T-cell with potent activity on both AML cell lines and primary patient-derived AML blasts in vitro while sparing healthy HSCs. Furthermore, in a disseminated mouse xenograft model using the CLL1-positive HL60 cell line, these CAR-T-cells completely eradicated tumor, thus supporting CLL1 as a promising target for CAR-T-cells to treat AML while limiting myelosuppressive toxicity.

Published
2017

4. Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446) from Thermotoga maritima at 1.77-A resolution

Author

Jeff Velasquez, Tanya Biorac, Adam Godzik, Peter Kuhn, Raymond C. Stevens, Guenter Wolf, Jie Ouyang, Heath E. Klock, Ross Floyd, Xiaoping Dai, Andreas Kreusch, Rebecca Page, Bill West, Keith O. Hodgson, Alyssa Robb, Hsiu-Ju Chiu, Jaume M. Canaves, Xianhong Wang, Scott A. Lesley, Linda S. Brinen, Andrew T. Morse, Juli Vincent, John S. Kovarik, Timothy M. McPhillips, Kin Moy, Marc-André Elsliger, Ashley M. Deacon, Mitchell D. Miller, Robert Schwarzenbacher, Ian A. Wilson, Frank von Delft, Eileen Ambing, Glen Spraggon, Mike DiDonato, Said Eshagi, Henry van den Bedem, Eric Hampton, Jamison Cambell, Eric Koesema, Carina Grittini, Kevin Quijano, Cathy Karlak, Polat Abdubek, Daniel McMullan, Inna Levin, John Wooley, Slawomir K. Grzechnik, Lukasz Jaroszewski, and Qingping Xu

Subjects
Models, Molecular, biology, Protein Conformation, Chemistry, Molecular Sequence Data, Resolution (electron density), Imidazoles, Reproducibility of Results, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Lyase, Biochemistry, Crystallography, Mutase, Structural Biology, Thermotoga maritima, Amino Acid Sequence, Crystallization, Intramolecular Transferases, Molecular Biology
Published
2016

5. Crystal structure of a putative PII-like signaling protein (TM0021) from Thermotoga maritima at 2.5 A resolution

Author

Jeff Velasquez, Mike DiDonato, Kevin Quijano, Xianhong Wang, Scott A. Lesley, Henry van den Bedem, Qingping Xu, Marc-André Elsliger, Polat Abdubek, Eric Hampton, Jie Ouyang, Timothy M. McPhillips, Xiaoping Dai, Jaume M. Canaves, Said Eshagi, Bill West, Guenter Wolf, Frank von Delft, Carina Grittini, Alyssa Robb, Lukasz Jaroszewski, Keith O. Hodgson, John Wooley, Andrew T. Morse, Mitchell D. Miller, Daniel McMullan, Inna Levin, Juli Vincent, H.-J. Chiu, Cathy Karlak, Robert Schwarzenbacher, Kin Moy, Slawomir K. Grzechnik, John S. Kovarik, Jamison Cambell, Eric Koesema, Peter Kuhn, Adam Godzik, Raymond C. Stevens, Tanja Biorac, Ross Floyd, Heath E. Klock, Linda S. Brinen, Andreas Kreusch, Rebecca Page, Glen Spraggon, Ashley M. Deacon, Ian A. Wilson, and Eileen Ambing

Subjects
Physics, Models, Molecular, biology, PII Nitrogen Regulatory Proteins, Resolution (electron density), Molecular Sequence Data, Synchrotron radiation, Reproducibility of Results, Particle accelerator, Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, law.invention, Crystallography, Bacterial Proteins, Structural Biology, law, Signaling proteins, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Signal Transduction
Published
2016
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6. Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 A resolution

Author

Lukasz Jaroszewski, Eric Hampton, Carina Grittini, Keith O. Hodgson, Tanya Biorac, Said Eshaghi, Adam Godzik, Kin Moy, Kevin Quijano, Marc-André Elsliger, Daniel McMullan, Inna Levin, Fred Rezezadeh, John Wooley, Alyssa Robb, Raymond C. Stevens, Frank von Delft, Guenter Wolf, Heath E. Klock, Timothy M. McPhillips, Qingping Xu, Andrew T. Morse, Juli Vincent, Linda S. Brinen, Xiaoping Dai, Cathy Karlak, Eric Sims, Slawomir K. Grzechnik, Mike DiDonato, Jaume M. Canaves, Polat Abdubek, Henry van den Bedem, Peter Kuhn, Jie Ouyang, Bill West, Xianhong Wang, Scott A. Lesley, Ross Floyd, Jeff Velasquez, Eric Koesema, Ron Reyes, Robert Schwarzenbacher, Mitchell D. Miller, Andreas Kreusch, Rebecca Page, Ashley M. Deacon, Ian A. Wilson, Eileen Ambing, and Glen Spraggon

Subjects
chemistry.chemical_classification, Models, Molecular, Binding Sites, Magnetic Resonance Spectroscopy, biology, Resolution (electron density), Molecular Sequence Data, Crystal structure, biology.organism_classification, Biochemistry, Protein Structure, Secondary, Crystallography, Enzyme, chemistry, Bacterial Proteins, Structural Biology, Structural Homology, Protein, Thermotoga maritima, Amino Acid Sequence, Crystallization, Molecular Biology, Conserved Sequence
Published
2016
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7. Crystal structure of an Udp-n-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga maritima at 2.3 A resolution

Author

Guenter Wolf, Peter Kuhn, Daniel McMullan, Inna Levin, Ross Floyd, Hsiu-Ju Chiu, Carina Grittini, John S. Kovarik, Ian A. Wilson, Eric Hampton, Kin Moy, Eileen Ambing, Glen Spraggon, Alyssa Robb, Jaume M. Canaves, Heath E. Klock, Kevin Quijano, John Wooley, Marc-André Elsliger, Andrew T. Morse, Timothy M. McPhillips, Bill West, Juli Vincent, Christian C. Lee, Polat Abdubek, Jie Ouyang, Frank von Delft, Xiaoping Dai, Jeff Velasquez, Linda S. Brinen, Slawomir K. Grzechnik, Tanya Biorac, Adam Godzik, Raymond C. Stevens, Jamison Cambell, Eric Koesema, Ashley M. Deacon, Andreas Kreusch, Rebecca Page, Xianhong Wang, Scott A. Lesley, Robert Schwarzenbacher, Mike DiDonato, Cathy Karlak, Henry van den Bedem, Qingping Xu, Keith O. Hodgson, Lukasz Jaroszewski, Said Eshagi, and Mitchell D. Miller

Subjects
Models, Molecular, chemistry.chemical_classification, DNA ligase, biology, Chemistry, Molecular Sequence Data, Resolution (electron density), Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Crystallography, Bacterial Proteins, UDP-N-acetylmuramate-alanine ligase, Structural Biology, Thermotoga maritima, Amino Acid Sequence, Peptide Synthases, Molecular Biology
Published
2016

8. Switch-mediated activation and retargeting of CAR-T cells for B-cell malignancies

Author

Vanessa Núñez, Oded Singer, Ashley K. Woods, Chan Hyuk Kim, David T. Rodgers, Ian R. Hardy, Feng Wang, Peter G. Schultz, Andrew D Schulman, Jennifer S. Y. Ma, Jiayin Shen, Travis S. Young, Eric Hampton, Yu Cao, Nitya S. Ramadoss, Magdalena Mazagova, Juanjuan Du, and Timothy M. Wright

Subjects
Cytotoxicity, Immunologic, 0301 basic medicine, Sialic Acid Binding Ig-like Lectin 2, medicine.medical_treatment, T-Cell Antigen Receptor Specificity, Mice, SCID, Lymphocyte Activation, Protein Engineering, Immunotherapy, Adoptive, Cell therapy, Mice, Cancer immunotherapy, Genes, Reporter, Mice, Inbred NOD, T-Lymphocyte Subsets, B-Lymphocytes, Multidisciplinary, Cytokine release syndrome, Basic-Leucine Zipper Transcription Factors, medicine.anatomical_structure, PNAS Plus, Cytokines, Female, Azides, Saccharomyces cerevisiae Proteins, Phenylalanine, Recombinant Fusion Proteins, Antigens, CD19, Genetic Vectors, Dose-Response Relationship, Immunologic, Receptors, Antigen, T-Cell, Biology, CD19, Structure-Activity Relationship, 03 medical and health sciences, Antigen, Antigens, Neoplasm, Cell Line, Tumor, Lymphopenia, Leukemia, B-Cell, medicine, Animals, Humans, B cell, medicine.disease, Xenograft Model Antitumor Assays, Molecular biology, Chimeric antigen receptor, Mice, Inbred C57BL, 030104 developmental biology, Cancer cell, Cancer research, biology.protein, human activities, Single-Chain Antibodies
Abstract

Chimeric antigen receptor T (CAR-T) cell therapy has produced impressive results in clinical trials for B-cell malignancies. However, safety concerns related to the inability to control CAR-T cells once infused into the patient remain a significant challenge. Here we report the engineering of recombinant antibody-based bifunctional switches that consist of a tumor antigen-specific Fab molecule engrafted with a peptide neo-epitope, which is bound exclusively by a peptide-specific switchable CAR-T cell (sCAR-T). The switch redirects the activity of the bio-orthogonal sCAR-T cells through the selective formation of immunological synapses, in which the sCAR-T cell, switch, and target cell interact in a structurally defined and temporally controlled manner. Optimized switches specific for CD19 controlled the activity, tissue-homing, cytokine release, and phenotype of sCAR-T cells in a dose-titratable manner in a Nalm-6 xenograft rodent model of B-cell leukemia. The sCAR-T-cell dosing regimen could be tuned to provide efficacy comparable to the corresponding conventional CART-19, but with lower cytokine levels, thereby offering a method of mitigating cytokine release syndrome in clinical translation. Furthermore, we demonstrate that this methodology is readily adaptable to targeting CD20 on cancer cells using the same sCAR-T cell, suggesting that this approach may be broadly applicable to heterogeneous and resistant tumor populations, as well as other liquid and solid tumor antigens.

Published
2016
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9. Crystal structure of MtnX phosphatase fromBacillus subtilisat 2.0 Å resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate

Author

Slawomir K. Grzechnik, Qingping Xu, Herbert L. Axelrod, Heath E. Klock, Aprilfawn White, Henry van den Bedem, John Wooley, Robert Schwarzenbacher, Guenter Wolf, Ian A. Wilson, Eric Koesema, Keith O. Hodgson, Justin Haugen, Polat Abdubek, Hsiu-Ju Chiu, Linda Okach, Sanjay Agarwalla, Christopher L. Rife, Ron Reyes, Andrew T. Morse, Eileen Ambing, Dennis Carlton, Sanjay Krishna, Mark W. Knuth, Mitchell D. Miller, Gye Won Han, Silvya Oommachen, Michael DiDonato, Marc-André Elsliger, Edward Nigoghossian, Eric Hampton, Lukasz Jaroszewski, Kumar Singh Saikatendu, Julie Feuerhelm, Jessica Paulsen, Thomas Clayton, Joanna Hale, Ashley M. Deacon, Adam Godzik, Daniel McMullan, Tamara Astakhova, Kevin K. Jin, Scott A. Lesley, and Lian Duan

Subjects
biology, Resolution (mass spectrometry), Chemistry, Stereochemistry, Hydrolysis, Molecular Sequence Data, Phosphatase, Crystal structure, Bacillus subtilis, Crystallography, X-Ray, biology.organism_classification, Phosphate, Biochemistry, Organophosphates, Phosphoric Monoester Hydrolases, chemistry.chemical_compound, Crystallography, Bacterial Proteins, Thioglycosides, Structural Biology, Hydrolase, Amino Acid Sequence, Molecular Biology
Published
2007
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10. Secreted PCSK9 promotes LDL receptor degradation independently of proteolytic activity

Author

Jennifer L. Harris, Christine Tumanut, Glen Spraggon, Gene Liau, Eric Hampton, Rachelle Tumanut, Scott A. Lesley, John Trauger, David Yowe, Julie-Ann Gavigan, Waan-Jeng Huang, Jun Li, and Ka Fai Suen

Subjects
Serine protease, Protease, biology, medicine.medical_treatment, PCSK9, Endoplasmic reticulum, Serine Endopeptidases, Subtilisin, Accelerated Publication, Cell Biology, Proprotein convertase, Biochemistry, Cell Line, Receptors, LDL, Zymogen, Mutation, Serine, medicine, biology.protein, Humans, Kexin, lipids (amino acids, peptides, and proteins), Molecular Biology
Abstract

PCSK9 (proprotein convertase subtilisin/kexin 9) is a secreted serine protease that regulates cholesterol homoeostasis by inducing post-translational degradation of hepatic LDL-R [LDL (low-density lipoprotein) receptor]. Intramolecular autocatalytic processing of the PCSK9 zymogen in the endoplasmic reticulum results in a tightly associated complex between the prodomain and the catalytic domain. Although the autocatalytic processing event is required for proper secretion of PCSK9, the requirement of proteolytic activity in the regulation of LDL-R is currently unknown. Co-expression of the prodomain and the catalytic domain in trans allowed for production of a catalytically inactive secreted form of PCSK9. This catalytically inactive PCSK9 was characterized and shown to be functionally equivalent to the wild-type protein in lowering cellular LDL uptake and LDL-R levels. These findings suggest that, apart from autocatalytic processing, the protease activity of PCSK9 is not necessary for LDL-R regulation.

Published
2007
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11. Crystal structure of homoserine O-succinyltransferase from Bacillus cereus at 2.4 Å resolution

Author

Lukasz Jaroszewski, Abhinav Kumar, John Wooley, Herbert L. Axelrod, Sanjay Agarwalla, Dennis Carlton, Adam Godzik, Marc-André Elsliger, Hsiu-Ju Chiu, Edward Nigoghossian, Dana Weekes, Daniel McMullan, Keith O. Hodgson, Justin Haugen, Ashley M. Deacon, Mitchell D. Miller, Henry van den Bedem, Mark W. Knuth, Polat Abdubek, Thomas Clayton, Christopher L. Rife, Heath E. Klock, Sanjay Krishna, Qingping Xu, Marc C. Deller, Joanna Hale, Slawomir K. Grzechnik, Scott A. Lesley, Ian A. Wilson, Tamara Astakhova, Lian Duan, Eileen Ambing, Ron Reyes, Kevin K. Jin, Aprilfawn White, Eric Koesema, Andrew T. Morse, Gye Won Han, Silvya Oommachen, Michael DiDonato, David Marciano, Eric Hampton, and Chloe Zubieta

Subjects
Models, Molecular, biology, Protein Conformation, Chemistry, Stereochemistry, Extramural, Molecular Sequence Data, Resolution (electron density), Bacillus cereus, Homoserine O-Succinyltransferase, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Haemophilus influenzae, Biochemistry, Microbiology, Bacterial Proteins, Structural Biology, Homoserine Transsuccinylase, Amino Acid Sequence, Dimerization, Molecular Biology
Published
2007
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12. The nuclear receptor LXR is a glucose sensor

Author

Nico Mitro, Enrique Saez, Eric Hampton, Andreas Kreusch, Leo Vargas, C. Godio, Puiying A. Mak, and Valentina Molteni

Subjects
Benzylamines, Snf3, medicine.medical_specialty, Transcription, Genetic, medicine.medical_treatment, Glucose-6-Phosphate, Receptors, Cytoplasmic and Nuclear, Carbohydrate metabolism, Biology, Ligands, Response Elements, Benzoates, digestive system, Mice, chemistry.chemical_compound, Cell Line, Tumor, Internal medicine, polycyclic compounds, medicine, Animals, Homeostasis, Humans, Glucose homeostasis, Liver X receptor, Liver X Receptors, Multidisciplinary, Glycogen, Insulin, Fatty Acids, Fasting, Lipid Metabolism, Orphan Nuclear Receptors, DNA-Binding Proteins, Cholesterol, Glucose, Retinoid X Receptors, Endocrinology, Gene Expression Regulation, Liver, Nuclear receptor, chemistry, Lipogenesis, lipids (amino acids, peptides, and proteins)
Abstract

The liver has a central role in glucose homeostasis, as it has the distinctive ability to produce and consume glucose. On feeding, glucose influx triggers gene expression changes in hepatocytes to suppress endogenous glucose production and convert excess glucose into glycogen or fatty acids to be stored in adipose tissue. This process is controlled by insulin, although debate exists as to whether insulin acts directly or indirectly on the liver. In addition to stimulating pancreatic insulin release, glucose also regulates the activity of ChREBP, a transcription factor that modulates lipogenesis. Here we describe another mechanism whereby glucose determines its own fate: we show that glucose binds and stimulates the transcriptional activity of the liver X receptor (LXR), a nuclear receptor that coordinates hepatic lipid metabolism. d-Glucose and d-glucose-6-phosphate are direct agonists of both LXR-alpha and LXR-beta. Glucose activates LXR at physiological concentrations expected in the liver and induces expression of LXR target genes with efficacy similar to that of oxysterols, the known LXR ligands. Cholesterol homeostasis genes that require LXR for expression are upregulated in liver and intestine of fasted mice re-fed with a glucose diet, indicating that glucose is an endogenous LXR ligand. Our results identify LXR as a transcriptional switch that integrates hepatic glucose metabolism and fatty acid synthesis.

Published
2006
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13. Crystal structure of the ApbE protein (TM1553) from Thermotoga maritima at 1.58 Å resolution

Author

Peter Kuhn, Raymond C. Stevens, Keith O. Hodgson, Sanjay Agarwalla, Jaume M. Canaves, Marc-André Elsliger, Edward Nigoghossian, Henry van den Bedem, Jie Ouyang, Michael DiDonato, Heath E. Klock, Mitchell D. Miller, Mark W. Knuth, Kevin Quijano, Robert Schwarzenbacher, Guenter Wolf, Eric Koesema, Kin Moy, Aprilfawn White, Gye Won Han, Polat Abdubek, Kevin K. Jin, Eric Hampton, Scott M. Brittain, Slawomir K. Grzechnik, Sanjay Krishna, Xianhong Wang, Bill West, Scott A. Lesley, Hsiu-Ju Chiu, Herbert L. Axelrod, Justin Haugen, Jeff Velasquez, Andrew T. Morse, Daniel McMullan, Adam Godzik, Christopher L. Rife, Lukasz Jaroszewski, Joanna Hale, Tamara Astakhova, Ron Reyes, Sylvia Oommachen, John Wooley, Qingping Xu, Andreas Kreusch, Glen Spraggon, Jessica Paulsen, Ashley M. Deacon, Krzysztof Ginalski, Ian A. Wilson, and Eileen Ambing

Subjects
Materials science, biology, Lipoproteins, Molecular Sequence Data, Resolution (electron density), Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Crystallography, Bacterial Proteins, Structural Biology, Thermotoga maritima, Amino Acid Sequence, Crystallization, Sequence Alignment, Molecular Biology
Published
2006
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14. Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 Å resolution

Author

Glen Spraggon, John Wooley, Jeff Velasquez, Kevin Quijano, Daniel McMullan, Inna Levin, Marc-André Elsliger, Slawomir K. Grzechnik, Edward Nigoghossian, Robert Schwarzenbacher, Ian A. Wilson, Guenter Wolf, Gye Won Han, Adam Godzik, Eileen Ambing, Keith O. Hodgson, Jaume M. Canaves, Ron Reyes, Carina Grittini, Mitchell D. Miller, Peter Kuhn, Henry van den Bedem, Ashley M. Deacon, Eric Hampton, Polat Abdubek, Lukasz Jaroszewski, Aprilfawn White, Justin Haugen, Jessica Paulsen, Eric Koesema, Qingping Xu, Hsiu-Ju Chiu, Andreas Kreusch, Joanna Hale, S. Sri Krishna, Scott A. Lesley, Irimpan I. Mathews, Raymond C. Stevens, Heath E. Klock, Kin Moy, and Michael DiDonato

Subjects
Models, Molecular, chemistry.chemical_classification, DNA ligase, Binding Sites, Molecular Sequence Data, Resolution (electron density), Crystal structure, Biology, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Phosphoribosylformylglycinamidine synthase, Protein Structure, Tertiary, Crystallography, chemistry, Structural Homology, Protein, Structural Biology, Thermotoga maritima, biology.protein, Amino Acid Sequence, Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor, Protein Structure, Quaternary, Molecular Biology, Image resolution
Published
2006
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15. Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 Å resolution

Author

Glen Spraggon, Ian A. Wilson, Eileen Ambing, Ashley M. Deacon, Guenter Wolf, Jessica Paulsen, Peter Kuhn, Michael Hornsby, Edward Nigoghossian, Henry van den Bedem, Linda Okach, John Wooley, Joanna Hale, Raymond C. Stevens, Daniel McMullan, Tanya Biorac, Adam Godzik, Mark W. Knuth, Kevin Quijano, Scott A. Lesley, Kin Moy, Julie Feuerhelm, Heath E. Klock, Ron Reyes, Polat Abdubek, Eric Hampton, Eric Koesema, Hsiu-Ju Chiu, Slawomir K. Grzechnik, Keith O. Hodgson, Aprilfawn White, Jeff Velasquez, Christopher L. Rife, S. Sri Krishna, M.A. Elsliger, Carina Grittini, Mitchell D. Miller, Herbert L. Axelrod, Justin Haugen, Michael DiDonato, Andreas Kreusch, Robert Schwarzenbacher, Sanjay Agarwalla, Qingping Xu, and Lukasz Jaroszewski

Subjects
Models, Molecular, HMG-box, Molecular Sequence Data, DNA, Single-Stranded, Crystal structure, Crystallography, X-Ray, Biochemistry, DNA-binding protein, Protein Structure, Secondary, chemistry.chemical_compound, Plasmid, Protein structure, X-Ray Diffraction, Structural Biology, Escherichia coli, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Peptide sequence, biology, biology.organism_classification, Mitochondria, DNA-Binding Proteins, Crystallography, chemistry, Anisotropy, DNA, Plasmids, Transcription Factors
Published
2006
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16. Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 Å resolution

Author

Slawomir K. Grzechnik, Gye Won Han, Michael DiDonato, Heath E. Klock, Sanjay Agarwalla, John Wooley, Robert Schwarzenbacher, Daniel McMullan, Hsiu-Ju Chiu, Guenter Wolf, Ron Reyes, Marc-André Elsliger, Lukasz Jaroszewski, Polat Abdubek, Edward Nigoghossian, Raymond C. Stevens, Eric Hampton, Ashley M. Deacon, Tanya Biorac, Adam Godzik, Jaume M. Canaves, Qingping Xu, Ian A. Wilson, Jeff Velasquez, Mitchell D. Miller, Justin Haugen, Aprilfawn White, Eric Koesema, Kin Moy, Jessica Paulsen, Peter Kuhn, Eileen Ambing, Glen Spraggon, Juli Vincent, Kevin Quijano, Joanna Hale, Carina Grittini, Christopher L. Rife, Andreas Kreusch, Scott A. Lesley, Michael Hornsby, Henry van den Bedem, Herbert L. Axelrod, and Keith O. Hodgson

Subjects
biology, Chemistry, Molecular Sequence Data, Zinc Fingers, Crystal structure, biology.organism_classification, Biochemistry, Crystallography, Bacterial Proteins, Structural Biology, Thermotoga maritima, Chaperone (protein), Hsp33, biology.protein, Amino Acid Sequence, Crystallization, Molecular Biology, Heat-Shock Proteins, Molecular Chaperones
Published
2005
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17. Crystal structure of the global regulatory protein CsrA from Pseudomonas putida at 2.05 Å resolution reveals a new fold

Author

Keith O. Hodgson, Marc-André Elsliger, Edward Nigoghossian, Aprilfawn White, Lukasz Jaroszewski, Michael Hornsby, Henry van den Bedem, Guenter Wolf, Slawomir K. Grzechnik, Gye Won Han, Qingping Xu, Tanya Biorac, Adam Godzik, Kevin Quijano, Raymond C. Stevens, Joanna Hale, Hsiu-Ju Chiu, Herbert L. Axelrod, Heath E. Klock, Jessica Paulsen, Mitchell D. Miller, Scott A. Lesley, Carina Grittini, John Wooley, Christopher L. Rife, Robert Schwarzenbacher, Daniel McMullan, Michael DiDonato, Justin Haugen, Ron Reyes, Polat Abdubek, Jeff Velasquez, Eric Koesema, Juli Vincent, Eric Hampton, Peter Kuhn, Andreas Kreusch, Ian A. Wilson, Eileen Ambing, Kin Moy, Jaume M. Canaves, Ashley M. Deacon, Glen Spraggon, and Eric Sims

Subjects
Models, Molecular, Regulation of gene expression, Protein Folding, biology, Pseudomonas putida, Chemistry, Molecular Sequence Data, RNA-Binding Proteins, RNA-binding protein, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Microbiology, Bacterial Proteins, Structural Biology, Amino Acid Sequence, Dimerization, Molecular Biology
Published
2005
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18. Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold

Author

Polat Abdubek, Slawomir K. Grzechnik, Scott A. Lesley, Raymond C. Stevens, Kevin Quijano, Michael Hornsby, Henry van den Bedem, Guenter Wolf, Marc-André Elsliger, Heath E. Klock, Edward Nigoghossian, Lukasz Jaroszewski, Keith O. Hodgson, Jie Ouyang, John Wooley, Justin Haugen, Jaume M. Canaves, Jessica Paulsen, Aprilfawn White, Daniel McMullan, Inna Levin, Eric Koesema, Peter Kuhn, Ashley M. Deacon, Mitchell D. Miller, Gye Won Han, Qingping Xu, Ian A. Wilson, Herbert L. Axelrod, Hsiu-Ju Chiu, Eileen Ambing, Glen Spraggon, Tanya Biorac, Adam Godzik, Ron Reyes, Joanna Hale, Juli Vincent, Carina Grittini, Irimpan I. Mathews, Kin Moy, Andreas Kreusch, Michael DiDonato, Robert Schwarzenbacher, Eric Hampton, and Jeff Velasquez

Subjects
Models, Molecular, Protein Folding, biology, Protein Conformation, Chemistry, Stereochemistry, Crystal structure, Isomerase, Crystallography, X-Ray, Ligands, biology.organism_classification, Biochemistry, Protein structure, Structural Biology, Thermotoga maritima, Transfer RNA, Solvents, Protein folding, Isomerases, Molecular Biology
Published
2005
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19. Crystal structure of a novel manganese-containing cupin (TM1459) from Thermotoga maritima at 1.65 Å resolution

Author

Keith O. Hodgson, Raymond C. Stevens, Guenter Wolf, Kevin Quijano, Alyssa Robb, Andrew T. Morse, Juli Vincent, Heath E. Klock, Adam Godzik, Eric Koesema, Marc-André Elsliger, Andreas Kreusch, Rebecca Page, Frank von Delft, Timothy M. McPhillips, Inna Levin, Lukasz Jaroszewski, Jaume M. Canaves, Carina Grittini, Eric Sims, Xianhong Wang, Qingping Xu, Scott A. Lesley, Ashley M. Deacon, Linda S. Brinen, Jeff Velasquez, Ron Reyes, Slawomir K. Grzechnik, Ian A. Wilson, Kin Moy, Mike DiDonato, Jie Ouyang, Said Eshagi, Fred Rezezadeh, Henry van den Bedem, Glen Spraggon, John S. Kovarik, John Wooley, Xiaoping Dai, Daniel McMullan, Peter Kuhn, Bill West, Eric Hampton, Ross Floyd, Cathy Karlak, Mitchell D. Miller, and Robert Schwarzenbacher

Subjects
Models, Molecular, Molecular Sequence Data, chemistry.chemical_element, Crystal structure, Manganese, Biochemistry, Protein Structure, Secondary, Bacterial protein, Protein structure, Bacterial Proteins, Structural Biology, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Binding Sites, biology, Chemistry, Resolution (electron density), biology.organism_classification, Protein Structure, Tertiary, Structural homology, Crystallography, Structural Homology, Protein, Multiprotein Complexes, Crystallization, Oxidoreductases
Published
2004
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20. Time-resolved fluorescence resonance energy transfer and surface plasmon resonance-based assays for retinoid and transthyretin binding to retinol-binding protein 4

Author

Paul Anderson, Edward Nigoghossian, Heath E. Klock, Mark W. Knuth, Eric Hampton, Tetsuo Uno, Orzala Sharif, Richard E. Trager, Huiyong Hu, Richard Glynne, Jason T. Matzen, Sassan M. Azarian, Jeremy S. Caldwell, and Achim Brinker

Subjects
Time Factors, medicine.drug_class, Biophysics, Retinoic acid, Drug Evaluation, Preclinical, Biochemistry, chemistry.chemical_compound, Retinoids, medicine, Fluorescence Resonance Energy Transfer, Humans, Prealbumin, Retinoid, Surface plasmon resonance, Molecular Biology, Retinol binding protein 4, biology, Molecular Structure, Chemistry, Ligand binding assay, Cell Biology, Surface Plasmon Resonance, Small molecule, Retinol binding protein, Fenretinide, biology.protein, Retinol-Binding Proteins, Plasma, Protein Binding
Abstract

Retinol-binding protein-4 (RBP4) is an emerging candidate drug target for type 2 diabetes and lipofuscin-mediated macular degeneration. The retinoic acid derivative fenretinide (N-(4-hydroxyphenyl) retinamide; HPR) exerts therapeutic effects in mouse models of obesity, diabetes, and Stargardt's disease by targeting RBP4. Fenretinide competes with retinoids for RBP4 binding, disrupts RBP4-transthyretin (TTR) complexes, and results in urinary secretion of RBP4 and systemic depletion of retinol. To enable the search for nonretinoid molecules with fenretinide-like activities we developed a HTS-compatible homogeneous TR-FRET assay monitoring the displacement of retinoic acid derivatives from RBP4 in high-density 384-well and 1536-well microtiter plate formats. The retinoid displacement assay proved to be highly sensitive and robust after miniaturization with IC(50)s for fenretinide and retinol ranging around 50 and 100 nM, respectively, and Z'-factors around 0.7. In addition, a surface plasmon resonance (SPR)-based secondary assay was developed to interrogate small molecule RBP4 binders for their ability to modulate the RBP4-TTR interaction. Finally, a 1.6 x 10(6) compound library was screened against the retinoid displacement assay. Several potent retinoid competitors were identified that also appeared to disrupt RBP4-TTR complexes. Some of these compounds could potentially serve as valuable tools to further probe RBP4 biology in the future.

Published
2009

21. The Thermotoga maritima Trk potassium transporter--from frameshift to function

Author

Scott A. Lesley, Hope A. Johnson, and Eric Hampton

Subjects
Rossmann fold, Potassium Channels, Protein subunit, Molecular Sequence Data, Biology, Microbiology, Protein structure, Adenosine Triphosphate, Bacterial Proteins, Escherichia coli, Thermotoga maritima, Amino Acid Sequence, Frameshift Mutation, Molecular Biology, Phylogeny, Binding Sites, Bacteria, Genetic Complementation Test, biology.organism_classification, Ligand (biochemistry), Enzymes and Proteins, Membrane protein, Biochemistry, Trk receptor, Potassium, Protein stabilization, Sequence Alignment, Protein Binding
Abstract

The gene for the Thermotoga maritima Trk potassium transporter component TrkA was originally thought to be a frameshift mutation and not to encode a functional protein. However, expression from this gene yielded a complex consisting of two distinct proteins designated TM1088A and -B. Genetic complementation of Escherichia coli mutants unable to transport potassium suggests that TM1088A/B is part of a functional Trk potassium transporter complex with the membrane protein TM1089. The protein structure for TM1088A shows a characteristic Rossmann fold indicating an NAD + binding site and has structural similarity to potassium channel-related proteins. Ligand binding studies indicated that ATP, ADP, and AMP stabilized TM1088A to a much greater degree than NADH and NAD, consistent with the crystal structure of TM1088A, which contains a bound AMP natural ligand at the characteristic GXGXXG nucleotide binding site. Mutation of single and all glycines at this nucleotide binding site eliminated in vitro protein stabilization by the ligand, yet these mutated proteins could still functionally complement the E. coli potassium uptake mutants. We predict that this new two-subunit class of TrkA proteins is present in a number of organisms. A further subclass of the predicted two-subunit TrkA proteins lack an identifiable membrane-spanning subunit of the Trk K + transporter. This class, as exemplified by Mycobacterium tuberculosis , did not complement E. coli potassium transport with the native E. coli TrkH; thus, it may require a novel TrkH-like protein for activity or provide an alternate function in vivo.

Published
2009

22. COSTS OF CALIFORNIA's CORRELATIVE RIGHTS DOCTRINE AS A SOLUTION TO GROUNDWATER OVERDRAFT

Author

Nathan Eric Hampton

Subjects
Economics and Econometrics, Public Administration, Present value, Overdrafting, Natural resource economics, General Business, Management and Accounting, Water trading, Water resources, Property rights, Development economics, Economics, San Joaquin, Adverse possession, Groundwater
Abstract

This paper reports the present value of groundwater use under alternative institutional structures for the eastern portion of California's San Joaquin Valley. The Gisser-Sanchez model, with data from the California Department of Water Resources, produced these results. The paper, through the use of an optimal control model, shows that private property rights outperform common property rights as an institutional guide to groundwater use. Furthermore, the paper shows that adjudicating groundwater rights under claim of adverse possession gives rise to a discounted flow of future income which, when compared with that of common property, gives the incentive to adjudicate groundwater rights.

Published
1990
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23. The self-inhibited structure of full-length PCSK9 at 1.9 A reveals structural homology with resistin within the C-terminal domain

Author

Jennifer L. Harris, Jun Li, Eric Hampton, Glen Spraggon, Scott A. Lesley, and Mark W. Knuth

Subjects
Models, Molecular, Saccharomyces cerevisiae Proteins, Structural similarity, Protein Conformation, Molecular Sequence Data, Static Electricity, Biology, Crystallography, X-Ray, Homology (biology), Protein Structure, Secondary, Protein structure, Catalytic Domain, Histidine, Resistin, Amino Acid Sequence, Cysteine, Disulfides, Peptide sequence, Genetics, Furin, Multidisciplinary, Binding Sites, Sequence Homology, Amino Acid, PCSK9, Serine Endopeptidases, Biological Sciences, Proprotein convertase, Protein Structure, Tertiary, Biochemistry, Models, Chemical, Mutation, Kexin, Proprotein Convertases, Proprotein Convertase 9, Baculoviridae, Oligopeptides
Abstract

Mutations in proprotein convertase subtilisin/kexin type 9 (PCSK9) are strongly associated with levels of low-density lipoprotein cholesterol in the blood plasma and, thereby, occurrence or resistance to atherosclerosis and coronary heart disease. Despite this importance, relatively little is known about the biology of PCSK9. Here, the crystal structure of a full-length construct of PCSK9 solved to 1.9-Å resolution is presented. The structure contains a fully folded C-terminal cysteine-rich domain (CRD), showing a distinct structural similarity to the resistin homotrimer, a small cytokine associated with obesity and diabetes. This structural relationship between the CRD of PCSK9 and the resistin family is not observed in primary sequence comparisons and strongly suggests a distant evolutionary link between the two molecules. This three-dimensional homology provides insight into the function of PCSK9 at the molecular level and will help to dissect the link between PCSK9 and CHD.

Published
2007

24. Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif

Author

Ron Reyes, Slawomir K. Grzechnik, Andrew T. Morse, Gye Won Han, Silvya Oommachen, Abhinav Kumar, Mark W. Knuth, Marc-André Elsliger, Edward Nigoghossian, Dennis Carlton, Ian A. Wilson, Qingping Xu, Piotr Kozbial, Eric Hampton, Paul Schimmel, Mitchell D. Miller, Adam Godzik, Herbert L. Axelrod, Chloe Zubieta, John Wooley, Daniel McMullan, Thomas Clayton, Eileen Ambing, Christopher L. Rife, Aprilfawn White, Keith O. Hodgson, Dana Weekes, Scott A. Lesley, Hsiu-Ju Chiu, Kevin K. Jin, Joanna Hale, Henry van den Bedem, Tamara Astakhova, Ashley M. Deacon, Lukasz Jaroszewski, Polat Abdubek, Sanjay Krishna, Mili Kapoor, Heath E. Klock, Linda Okach, Julie Feuerhelm, Marc C. Deller, David Marciano, and Lian Duan

Subjects
Protein Folding, Shewanella, Heme binding, Amino Acid Motifs, Molecular Sequence Data, Heme, Random hexamer, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, chemistry.chemical_compound, Bacterial Proteins, Structural Biology, Multienzyme Complexes, Catalytic Domain, Bacteroides, Amino Acid Sequence, Shewanella oneidensis, Coloring Agents, Molecular Biology, Conserved Sequence, Dye decolorizing peroxidase, biology, Chemistry, Active site, Isothermal titration calorimetry, biology.organism_classification, A-site, Crystallography, Peroxidases, biology.protein, Protein Binding
Abstract

BtDyP from Bacteroides thetaiotaomicron (strain VPI-5482) and TyrA from Shewanella oneidensis are dye-decolorizing peroxidases (DyPs), members of a new family of heme-dependent peroxidases recently identified in fungi and bacteria. Here, we report the crystal structures of BtDyP and TyrA at 1.6 and 2.7 Angstroms, respectively. BtDyP assembles into a hexamer, while TyrA assembles into a dimer; the dimerization interface is conserved between the two proteins. Each monomer exhibits a two-domain, {alpha}+{beta} ferredoxin-like fold. A site for heme binding was identified computationally, and modeling of a heme into the proposed active site allowed for identification of residues likely to be functionally important. Structural and sequence comparisons with other DyPs demonstrate a conservation of putative heme-binding residues, including an absolutely conserved histidine. Isothermal titration calorimetry experiments confirm heme binding, but with a stoichiometry of 0.3:1 (heme:protein).

Published
2007

25. Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 angstroms resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases

Author

Ashley M. Deacon, Ian A. Wilson, Lutz Tautz, Eileen Ambing, Andrew T. Morse, Michael DiDonato, Justin Haugen, Dennis Carlton, Polat Abdubek, Slawomir K. Grzechnik, Thomas Clayton, Tomas Mustelin, Ron Reyes, Eric Koesema, Gye Won Han, Sanjay Krishna, Silvya Oommachen, Joanna Hale, Mark W. Knuth, John Wooley, Mitchell D. Miller, Aprilfawn White, Tamara Astakhova, Christopher L. Rife, Heath E. Klock, Kevin K. Jin, Lukasz Jaroszewski, Daniel McMullan, Scott A. Lesley, Qingping Xu, Dana Weekes, Eric Hampton, Lian Duan, Marc-André Elsliger, Edward Nigoghossian, Hsiu-Ju Chiu, Henry van den Bedem, Adam Godzik, Herbert L. Axelrod, and Keith O. Hodgson

Subjects
Scaffold, Binding Sites, Chemistry, Neisseria meningitidis, Phosphatase, Resolution (electron density), Amino Acid Motifs, Molecular Sequence Data, Crystal structure, medicine.disease_cause, Crystallography, X-Ray, Biochemistry, Phosphoric Monoester Hydrolases, Protein Structure, Secondary, Bacterial Proteins, Structural Biology, Hydrolase, medicine, Amino Acid Sequence, Molecular Biology
Published
2007

26. Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution

Author

Daniel McMullan, Inna Levin, Hope A. Johnson, Ian A. Wilson, Scott A. Lesley, Herbert L. Axelrod, Eileen Ambing, Gye Won Han, Marc Fasnacht, Eric Sims, Silvya Oommachen, Tamara Astakhova, Glen Spraggon, Andreas Kreusch, Keith O. Hodgson, Ron Reyes, Rebecca Page, Justin Haugen, Mitchell D. Miller, Thomas Clayton, Sanjay Agarwalla, Mickey Kosloff, Vandana Sridhar, Jaume M. Canaves, Dennis Carlton, Polat Abdubek, Sanjay Krishna, Henry van den Bedem, Heath E. Klock, Raymond C. Stevens, Hsiu-Ju Chiu, Peter Kuhn, Eric Hampton, Slawomir K. Grzechnik, Robert Schwarzenbacher, Guenter Wolf, Christopher L. Rife, Joanna Hale, Carina Grittini, Ashley M. Deacon, Marc-André Elsliger, Edward Nigoghossian, Mark W. Knuth, Kevin Quijano, John Wooley, Eric Koesema, Aprilfawn White, Julie Feuerhelm, Adam Godzik, Qingping Xu, Andrew T. Morse, Lian Duan, Kin Moy, Kevin K. Jin, Michael DiDonato, Jeff Velasquez, Lukasz Jaroszewski, Linda Okach, and Jessica Paulsen

Subjects
Models, Molecular, Molecular Sequence Data, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Structural genomics, Bacterial Proteins, Structural Biology, Phylogenetics, Consensus sequence, Transferase, Amino Acid Sequence, Molecular Biology, Peptide sequence, Phylogeny, Glutathione Transferase, chemistry.chemical_classification, biology, Agrobacterium tumefaciens, Protein engineering, biology.organism_classification, Enzyme, chemistry, Dimerization
Abstract

Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.

Published
2006

27. Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 A resolution reveals a fold similar to the Ran-binding protein Mog1p

Author

Andreas Kreusch, Heath E. Klock, Marc-André Elsliger, Jaume M. Canaves, Edward Nigoghossian, Slawomir K. Grzechnik, Henry van den Bedem, Lukasz Jaroszewski, Justin Haugen, Guenter Wolf, Ron Reyes, Andrew T. Morse, Ashley M. Deacon, Hsiu-Ju Chiu, Thomas Clayton, Ian A. Wilson, Mark W. Knuth, Michael DiDonato, Kevin Quijano, John Wooley, Joanna Hale, Peter Kuhn, Kevin K. Jin, Eileen Ambing, Qingping Xu, Lian Duan, Glen Spraggon, Adam Godzik, Christopher L. Rife, Herbert L. Axelrod, Eric Koesema, Tamara Astakhova, Sanjay Agarwalla, Eric Hampton, Julie Feuerhelm, Gye Won Han, Silvya Oommachen, Dennis Carlton, Keith O. Hodgson, Scott A. Lesley, Robert Schwarzenbacher, Polat Abdubek, Sanjay Krishna, Linda Okach, Mitchell D. Miller, Daniel McMullan, Raymond C. Stevens, Aprilfawn White, and Jessica Paulsen

Subjects
Physics, Models, Molecular, Protein Folding, Saccharomyces cerevisiae Proteins, biology, Molecular Sequence Data, Fold (geology), Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, Protein tertiary structure, Protein Structure, Secondary, ran GTP-Binding Protein, Ran-binding protein, Bacterial Proteins, Structural Biology, Signaling proteins, Thermotoga maritima, Amino Acid Sequence, Molecular Biology
Published
2006

28. Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6 A resolution reveals a new fold with a novel active site

Author

Lian Duan, Guenter Wolf, Polat Abdubek, Sanjay Krishna, Daniel McMullan, Inna Levin, Keith O. Hodgson, Jessica Paulsen, Jaume M. Canaves, Mark W. Knuth, Kevin Quijano, Joanna Hale, Linda Okach, Michael DiDonato, Andreas Kreusch, Hsiu-Ju Chiu, Sanjay Agarwalla, Marc-André Elsliger, Mitchell D. Miller, Edward Nigoghossian, Scott A. Lesley, Q. Xu, Heath E. Klock, Eric Hampton, Glen Spraggon, Herbert L. Axelrod, Henry van den Bedem, Adam Godzik, Lukasz Jaroszewski, Peter Kuhn, John Wooley, Justin Haugen, Ron Reyes, Robert Schwarzenbacher, Raymond C. Stevens, Eric Koesema, Aprilfawn White, Slawomir K. Grzechnik, Ian A. Wilson, Eileen Ambing, Silvya Oommachen, Scott M. Brittain, Christopher L. Rife, Andrew T. Morse, Ashley M. Deacon, and Kevin K. Jin

Subjects
Models, Molecular, Protein Folding, Binding Sites, Protein Conformation, media_common.quotation_subject, Acid Phosphatase, Molecular Sequence Data, Art, Crystallography, X-Ray, Biochemistry, Structural Biology, 2-phosphosulfolactate phosphatase, Clostridium acetobutylicum, Amino Acid Sequence, Molecular Biology, Humanities, media_common
Abstract

Michael DiDonato, S. Sri Krishna, Robert Schwarzenbacher, Daniel McMullan, Sanjay Agarwalla, Scott M. Brittain, Mitchell D. Miller, Polat Abdubek, Eileen Ambing, Herbert L. Axelrod, JaumeM. Canaves, Hsiu-Ju Chiu, Ashley M. Deacon, Lian Duan, Marc-Andre Elsliger, Adam Godzik, Slawomir K. Grzechnik, Joanna Hale, Eric Hampton, Justin Haugen, Lukasz Jaroszewski, Kevin K. Jin, Heath E. Klock, Mark W. Knuth, Eric Koesema, Andreas Kreusch, Peter Kuhn, Scott A. Lesley, Inna Levin, Andrew T. Morse, Edward Nigoghossian, Linda Okach, Silvya Oommachen, Jessica Paulsen, Kevin Quijano, Ron Reyes, Christopher L. Rife, Glen Spraggon, Raymond C. Stevens, Henry van den Bedem, AprilfawnWhite, Guenter Wolf, Qingping Xu, Keith O. Hodgson, John Wooley, and Ian A. Wilson* The Joint Center for Structural Genomics Stanford Synchrotron Radiation Laboratory, Stanford University, Menlo Park, California The University of California, San Diego, La Jolla, California The Genomics Institute of the Novartis Research Foundation, San Diego, California The Scripps Research Institute, La Jolla, California

Published
2006

29. Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) from Thermotoga maritima at 1.90 A resolution

Author

Glen Spraggon, Aprilfawn White, Lian Duan, Edward Nigoghossian, Sanjay Agarwalla, Andrew T. Morse, Dennis Carlton, Slawomir K. Grzechnik, Guenter Wolf, Adam Godzik, Marc-André Elsliger, Raymond C. Stevens, Sanjay Krishna, Keith O. Hodgson, Silvya Oommachen, John S. Kovarik, Polat Abdubek, Ian A. Wilson, Ron Reyes, Jaume M. Canaves, Christopher L. Rife, Eileen Ambing, Peter Kuhn, Hsiu-Ju Chiu, John Wooley, Jessica Paulsen, Kevin Quijano, Justin Haugen, Eric Hampton, Linda Okach, Inna Levin, Herbert L. Axelrod, Ashley M. Deacon, Michael Didonato, Henry van den Bedem, Eric Koesema, Scott A. Lesley, Kevin K. Jin, Daniel McMullan, Irimpan I. Mathews, Lukasz Jaroszewski, Robert Schwarzenbacher, Qingping Xu, Heath E. Klock, Andreas Kreusch, Mitchell D. Miller, Thomas Clayton, and Joanna Hale

Subjects
chemistry.chemical_classification, DNA ligase, biology, ATP synthase, Stereochemistry, Chemistry, Protein subunit, Resolution (electron density), Molecular Sequence Data, Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, Protein structure, Bacterial Proteins, Structural Biology, Thermotoga maritima, biology.protein, Amino Acid Sequence, Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor, Crystallization, Protein Structure, Quaternary, Molecular Biology, Peptide sequence
Published
2006

30. Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 angstrom resolution

Author

Justin Haugen, Joanna Hale, John Wooley, Aprilfawn White, Daniel McMullan, Sanjay Agarwalla, Peter Kuhn, Robert Schwarzenbacher, Guenter Wolf, Jessica Paulsen, Ron Reyes, Andreas Kreusch, Mark W. Knuth, Kevin Quijano, Raymond C. Stevens, Kin Moy, Scott A. Lesley, Jaume M. Canaves, Qingping Xu, Slawomir K. Grzechnik, Mitchell D. Miller, Gye Won Han, Lukasz Jaroszewski, Polat Abdubek, Sanjay Krishna, Carina Grittini, Christopher L. Rife, Michael DiDonato, Heath E. Klock, Eric Koesema, Eric Hampton, Michael Hornsby, Henry van den Bedem, Hsiu-Ju Chiu, Keith O. Hodgson, Marc-André Elsliger, Ashley M. Deacon, Edward Nigoghossian, Jeff Velasquez, Glen Spraggon, Herbert L. Axelrod, Tanya Biorac, Adam Godzik, Ian A. Wilson, and Eileen Ambing

Subjects
chemistry.chemical_classification, Models, Molecular, Binding Sites, Molecular Structure, Stereochemistry, Resolution (electron density), Molecular Sequence Data, Crystal structure, Biochemistry, Protein Structure, Secondary, Dioxygenases, Protein Structure, Tertiary, Mice, Acireductone dioxygenase, chemistry, Structural Biology, Oxidoreductase, Metals, Animals, Amino Acid Sequence, Crystallization, Databases, Protein, Molecular Biology, Protein Binding
Published
2006

31. Crystal structure of TM1367 from Thermotoga maritima at 1.90 A resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold

Author

Raymond C. Stevens, Lukasz Jaroszewski, John Wooley, Carina Grittini, Scott A. Lesley, Qingping Xu, Aprilfawn White, Ron Reyes, Adam Godzik, Ashley M. Deacon, Hsiu-Ju Chiu, Marc-André Elsliger, Edward Nigoghossian, Justin Haugen, Daniel McMullan, Joanna Hale, Eric Hampton, Michael Hornsby, Henry van den Bedem, Peter Kuhn, Polat Abdubek, Christopher L. Rife, Julie Feuerhelm, Sanjay Krishna, Slawomir K. Grzechnik, Heath E. Klock, Jaume M. Canaves, Keith O. Hodgson, Kevin K. Jin, Herbert L. Axelrod, Ian A. Wilson, Robert Schwarzenbacher, Gye Won Han, Silvya Oommachen, Guenter Wolf, Eileen Ambing, Glen Spraggon, Eric Koesema, Mitchell D. Miller, Kin Moy, Jeff Velasquez, Mark W. Knuth, Kevin Quijano, Andreas Kreusch, Michael DiDonato, Sanjay Agarwalla, Jessica Paulsen, and Linda Okach

Subjects
Models, Molecular, Protein Folding, Molecular Sequence Data, Crystal structure, Crystallography, X-Ray, Biochemistry, Polyethylene Glycols, Cyclophilins, Bacterial Proteins, Structural Biology, Humans, Thermotoga maritima, Amino Acid Sequence, Protein Structure, Quaternary, Molecular Biology, Cyclophilin, Peptidylprolyl isomerase, Binding Sites, biology, Chemistry, Fold (geology), Peptidylprolyl Isomerase, biology.organism_classification, Protein Structure, Tertiary, Crystallography
Published
2006

32. Crystal structure of virulence factor CJ0248 from Campylobacter jejuni at 2.25 A resolution reveals a new fold

Author

Glen Spraggon, Lukasz Jaroszewski, Robert Schwarzenbacher, Michael DiDonato, Guenter Wolf, Raymond C. Stevens, Christopher L. Rife, Hsiu-Ju Chiu, Carina Grittini, Kin Moy, Marc-André Elsliger, Ashley M. Deacon, Edward Nigoghossian, Andreas Kreusch, Jessica Paulsen, Kevin Quijano, Jaume M. Canaves, Aprilfawn White, Sanjay Agarwalla, Ian A. Wilson, Herbert L. Axelrod, Tanya Biorac, Adam Godzik, Gye Won Han, Scott A. Lesley, Eileen Ambing, Ron Reyes, Keith O. Hodgson, Eric Hampton, Slawomir K. Grzechnik, Jeff Velasquez, John Wooley, Michael Hornsby, Henry van den Bedem, Eric Koesema, Daniel McMullan, Polat Abdubek, Joanna Hale, Mitchell D. Miller, Heath E. Klock, Peter Kuhn, Justin Haugen, and Qingping Xu

Subjects
Physics, Models, Molecular, Protein Folding, biology, Virulence Factors, Fold (geology), Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, Campylobacter jejuni, Virulence factor, Protein Structure, Secondary, Bacterial protein, Bacterial Proteins, Structural Biology, Protein folding, Molecular Biology
Published
2005

33. Crystal structure of a conserved hypothetical protein (gi: 13879369) from Mouse at 1.90 A resolution reveals a new fold

Author

Ian A. Wilson, Eileen Ambing, Ashley M. Deacon, Andreas Kreusch, Jeff Velasquez, Jessica Paulsen, Juli Vincent, Hsiu-Ju Chiu, Herbert L. Axelrod, Polat Abdubek, Michael DiDonato, Gye Won Han, Carina Grittini, Jaume M. Canaves, Raymond C. Stevens, Guenter Wolf, Qingping Xu, Heath E. Klock, Slawomir K. Grzechnik, Michael Hornsby, Christopher L. Rife, Henry van den Bedem, Scott A. Lesley, Kevin Quijano, Marc-André Elsliger, Peter Kuhn, Edward Nigoghossian, Keith O. Hodgson, Aprilfawn White, Joanna Hale, Tanya Biorac, Adam Godzik, Eric Hampton, Mitchell D. Miller, Eric Koesema, Justin Haugen, Eric Sims, John Wooley, Ron Reyes, Daniel McMullan, Robert Schwarzenbacher, Kin Moy, Lukasz Jaroszewski, and Glen Spraggon

Subjects
Models, Molecular, Protein Folding, Chemistry, Hypothetical protein, Proteins, Fold (geology), Crystal structure, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Molecular Weight, Crystallography, Mice, Open Reading Frames, Structural Biology, Transferase, Animals, Databases, Protein, Molecular Biology, Conserved Sequence
Published
2005

34. Crystal structure of a putative modulator of DNA gyrase (pmbA) from Thermotoga maritima at 1.95 A resolution reveals a new fold

Author

Peter Kuhn, Kevin Quijano, Slawomir K. Grzechnik, Marc-André Elsliger, Ian A. Wilson, Justin Haugen, Polat Abdubek, Edward Nigoghossian, Aprilfawn White, Eileen Ambing, John Wooley, Glen Spraggon, Kin Moy, Carina Grittini, Robert Schwarzenbacher, Daniel McMullan, Heath E. Klock, Hsiu-Ju Chiu, Raymond C. Stevens, Ashley M. Deacon, Guenter Wolf, Mitchell D. Miller, Ron Reyes, Joanna Hale, Jessica Paulsen, Eric Koesema, Gye Won Han, Scott A. Lesley, Andreas Kreusch, Lukasz Jaroszewski, Tanya Biorac, Adam Godzik, Juli Vincent, Qingping Xu, Keith O. Hodgson, Michael Hornsby, Henry van den Bedem, Eric Sims, Herbert L. Axelrod, Michael DiDonato, Jeff Velasquez, Christopher L. Rife, Eric Hampton, and Jaume M. Canaves

Subjects
Regulation of gene expression, Models, Molecular, Protein Folding, biology, Chemistry, Stereochemistry, Molecular Sequence Data, Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, DNA gyrase, Bacterial Proteins, Structural Biology, DNA Gyrase, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Dimerization
Published
2005

35. Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution

Author

John Wooley, Justin Haugen, Peter Kuhn, Heath E. Klock, Scott A. Lesley, Joanna Hale, Hsiu-Ju Chiu, Guenter Wolf, Tanya Biorac, Adam Godzik, Qingping Xu, Xiaoping Dai, Polat Abdubek, Slawomir K. Grzechnik, Ron Reyes, Glen Spraggon, Michael DiDonato, Eric Koesema, Carina Grittini, Gye Won Han, Raymond C. Stevens, Marc-André Elsliger, Jeff Velasquez, Edward Nigoghossian, Daniel McMullan, Mitchell D. Miller, Kevin Quijano, Keith O. Hodgson, Aprilfawn White, Robert Schwarzenbacher, Eric Hampton, Juli Vincent, Kin Moy, Lukasz Jaroszewski, Ian A. Wilson, Herbert L. Axelrod, Michael Hornsby, Henry van den Bedem, Eileen Ambing, Ashley M. Deacon, Jessica Paulsen, Jaume M. Canaves, Andreas Kreusch, and Timothy M. McPhillips

Subjects
Models, Molecular, Messenger RNA, Chemistry, Resolution (electron density), DCPS, Molecular Sequence Data, RNA-binding protein, Crystal structure, Crystallography, X-Ray, Biochemistry, Sensitivity and Specificity, Protein Structure, Secondary, Mice, Apoenzymes, Structural Biology, Endoribonucleases, Animals, Amino Acid Sequence, RNA, Messenger, Molecular Biology, Decapping enzyme
Published
2005

36. Crystal structure of an indigoidine synthase A (IndA)-like protein (TM1464) from Thermotoga maritima at 1.90 A resolution reveals a new fold

Author

Jaume M. Canaves, Slawomir K. Grzechnik, Peter Kuhn, Heath E. Klock, Lukasz Jaroszewski, Jie Ouyang, Ron Reyes, Raymond C. Stevens, John Wooley, Keith O. Hodgson, Olga Zagnitko, Kin Moy, Polat Abdubek, Guenter Wolf, Andreas Kreusch, Rebecca Page, Jeff Velasquez, Glen Spraggon, Michael DiDonato, Joanna Hale, Xianhong Wang, Scott A. Lesley, Qingping Xu, Mitchell D. Miller, Cathy Karlak, Michael Hornsby, Henry van den Bedem, Daniel McMullan, Inna Levin, Alyssa Robb, Kevin Quijano, Bill West, Eric Sims, Eric Hampton, Andrew T. Morse, Juli Vincent, Jamison Cambell, Eric Koesema, Justin Haugen, Robert Schwarzenbacher, Ashley M. Deacon, Carina Grittini, Ian A. Wilson, Hsiu-Ju Chiu, Eileen Ambing, Marc-André Elsliger, Edward Nigoghossian, Tanya Biorac, Adam Godzik, and Gye Won Han

Subjects
Models, Molecular, Protein Folding, biology, ATP synthase, Chemistry, Stereochemistry, Protein Conformation, Fold (geology), Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, Bacterial Proteins, Structural Biology, Thermotoga maritima, biology.protein, Molecular Biology, Indigoidine, Piperidones
Published
2005

37. Crystal structure of an alanine-glyoxylate aminotransferase from Anabaena sp. at 1.70 A resolution reveals a noncovalently linked PLP cofactor

Author

Guenter Wolf, Gye Won Han, Kin Moy, Kevin Quijano, Slawomir K. Grzechnik, Michael Hornsby, Henry van den Bedem, Andreas Kreusch, Jessica Paulsen, Heath E. Klock, Polat Abdubek, Hsiu-Ju Chiu, Rebecca Page, Qingping Xu, Ron Reyes, Marc-André Elsliger, Peter Kuhn, Edward Nigoghossian, Eric Hampton, Andrew T. Morse, Jeff Velasquez, Frank von Delft, Juli Vincent, Lukasz Jaroszewski, Tanya Biorac, Adam Godzik, Olga Zagnitko, Michael DiDonato, Daniel McMullan, Inna Levin, Carina Grittini, Bill West, Keith O. Hodgson, Joanna Hale, Xiaoping Dai, Eric Koesema, Mitchell D. Miller, Justin Haugen, John Wooley, Xianhong Wang, Scott A. Lesley, Timothy M. McPhillips, Ashley M. Deacon, Glen Spraggon, Eric Sims, Robert Schwarzenbacher, Ian A. Wilson, Eileen Ambing, Jie Ouyang, Raymond C. Stevens, Jaume M. Canaves, and Aprilfawn White

Subjects
Models, Molecular, Protein Conformation, Stereochemistry, Molecular Sequence Data, Anabaena sp, Alanine glyoxylate aminotransferase, Electrons, Crystal structure, Crystallography, X-Ray, Biochemistry, Cofactor, Structural Biology, Humans, Transferase, Amino Acid Sequence, Molecular Biology, Transaminases, Sequence Homology, Amino Acid, biology, Chemistry, Resolution (electron density), Proteins, Stereoisomerism, Anabaena, Protein Structure, Tertiary, biology.protein
Published
2005

38. Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution

Author

Timothy M. McPhillips, Eric Sims, Eric Hampton, Xiaoping Dai, Jaume M. Canaves, John Wooley, Aprilfawn White, Carina Grittini, Slawomir K. Grzechnik, Daniel McMullan, Inna Levin, Joanna Hale, Heath E. Klock, Lukasz Jaroszewski, Peter Kuhn, Keith O. Hodgson, Justin Haugen, Olga Zagnitko, Guenter Wolf, Kevin Quijano, Kin Moy, Hsiu-Ju Chiu, W. Peti, Joseph W. Arndt, Qingping Xu, Polat Abdubek, Mitchell D. Miller, Andrew T. Morse, Jeff Velasquez, Juli Vincent, Bill West, Jie Ouyang, Marc-André Elsliger, Gye Won Han, Edward Nigoghossian, Andreas Kreusch, Michael Hornsby, Henry van den Bedem, Rebecca Page, Robert Schwarzenbacher, Michael Didonato, Eric Koesema, Frank von Delft, Xianhong Wang, Scott A. Lesley, Ashley M. Deacon, Glen Spraggon, Raymond C. Stevens, Ian A. Wilson, Eileen Ambing, Ron Reyes, Tanya Biorac, and Adam Godzik

Subjects
Models, Molecular, Saccharomyces cerevisiae Proteins, Hydrolases, Protein Conformation, Molecular Sequence Data, Saccharomyces cerevisiae, Molecular Conformation, Alpha (ethology), Crystal structure, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Structural Biology, Hydrolase, Serine, Amino Acid Sequence, Beta (finance), Molecular Biology, Binding Sites, biology, Chemistry, Resolution (electron density), Computational Biology, Serine hydrolase, biology.organism_classification, Protein Structure, Tertiary, Software
Published
2005

39. Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold

Author

Keith O. Hodgson, Kin Moy, Jie Ouyang, Polat Abdubek, Guenter Wolf, Heath E. Klock, Hsiu-Ju Chiu, Xiaoping Dai, Mitchell D. Miller, Marc-André Elsliger, Frank von Delft, Robert Schwarzenbacher, Michael Hornsby, Henry van den Bedem, Carina Grittini, Jeff Velasquez, Tanya Biorac, Adam Godzik, Lukasz Jaroszewski, Olga Zagnitko, Eric Sims, Raymond C. Stevens, Qingping Xu, Eric Koesema, Andreas Kreusch, Michael DiDonato, Rebecca Page, Bill West, Jaume M. Canaves, Peter Kuhn, Aprilfawn White, Daniel McMullan, Inna Levin, Alyssa Robb, Andrew T. Morse, Juli Vincent, Eric Hampton, Ian A. Wilson, Slawomir K. Grzechnik, Xianhong Wang, Scott A. Lesley, Eileen Ambing, Ashley M. Deacon, Glen Spraggon, John Wooley, Kevin Quijano, and Ron Reyes

Subjects
Models, Molecular, Ammonia-Lyases, Stereochemistry, Protein Conformation, Molecular Sequence Data, Molecular Conformation, Crystal structure, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Formiminotetrahydrofolate cyclodeaminase, Structural Biology, Enzyme Stability, Thermotoga maritima, Amino Acid Sequence, Molecular Biology, Binding Sites, biology, Chemistry, Fold (geology), Lyase, biology.organism_classification, Protein Structure, Tertiary, Models, Chemical, Crystallization
Published
2005

40. Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 A resolution

Author

Jaume M. Canaves, Timothy M. McPhillips, Kevin Quijano, Linda S. Brinen, Mitchell D. Miller, Peter Kuhn, Polat Abdubek, Ross Floyd, Mike DiDonato, John Wooley, Guenter Wolf, Jamison Cambell, Eric Koesema, Marc-André Elsliger, Raymond C. Stevens, Carina Grittini, Daniel McMullan, Inna Levin, Xiaoping Dai, Henry van den Bedem, Said Eshagi, Cathy Karlak, Alyssa Robb, Andrew T. Morse, Juli Vincent, Kin Moy, Jie Ouyang, Slawomir K. Grzechnik, Andreas Kreusch, Rebecca Page, Bill West, Frank von Delft, Keith O. Hodgson, Heath E. Klock, Hsiu-Ju Chiu, Robert Schwarzenbacher, Xianhong Wang, Scott A. Lesley, John S. Kovarik, Jeff Velasquez, Lukasz Jaroszewski, Qingping Xu, Eric Hampton, Tanya Biorac, Adam Godzik, Ashley M. Deacon, Ian A. Wilson, Eileen Ambing, and Glen Spraggon

Subjects
Models, Molecular, Crystallography, biology, Tandem, Resolution (electron density), Molecular Sequence Data, CBS domain, Cystathionine beta-Synthase, Crystal structure, biology.organism_classification, Biochemistry, Cystathionine beta synthase, Protein Structure, Secondary, Protein Structure, Tertiary, Bacterial Proteins, Structural Biology, Thermotoga maritima, biology.protein, Transferase, Amino Acid Sequence, Molecular Biology
Published
2004

41. Crystal structure of an allantoicase (YIR029W) from Saccharomyces cerevisiae at 2.4 A resolution

Author

Lukasz Jaroszewski, Alyssa Robb, Glen Spraggon, John Wooley, Andrew T. Morse, Jie Ouyang, Juli Vincent, Qingping Xu, Jaume M. Canaves, John S. Kovarik, Slawomir K. Grzechnik, Jamison Cambell, Eric Koesema, Mitchell D. Miller, Guenter Wolf, Linda S. Brinen, Daniel McMullan, Bill West, Xianhong Wang, Scott A. Lesley, Eric Hampton, Fred Rezezadeh, Raymond C. Stevens, Inna Levin, Timothy M. McPhillips, Heath E. Klock, Ian A. Wilson, Eric Sims, Mike DiDonato, Jeff Velasquez, Carina Grittini, Peter Kuhn, Eileen Ambing, Henry van den Bedem, Andreas Kreusch, Rebecca Page, Cathy Karlak, Ross Floyd, Robert Schwarzenbacher, Keith O. Hodgson, Ashley M. Deacon, Xiaoping Dai, Kevin Quijano, Kin Moy, Polat Abdubek, Ron Reyes, Tanya Biorac, Adam Godzik, Marc-André Elsliger, Frank von Delft, and Hsiu-Ju Chiu

Subjects
Models, Molecular, biology, Chemistry, Molecular Sequence Data, Resolution (electron density), Saccharomyces cerevisiae, Crystal structure, Crystallography, X-Ray, biology.organism_classification, Biochemistry, Protein Structure, Secondary, Ureohydrolases, Protein Structure, Tertiary, Multienzyme Complexes, Structural Homology, Protein, Structural Biology, Hydrolase, Allantoicase, Amino Acid Sequence, Molecular Biology, Conserved Sequence
Published
2004

42. Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution

Author

Andreas Kreusch, Rebecca Page, Qingping Xu, Henry van den Bedem, Carina Grittini, Xiaoping Dai, Raymond C. Stevens, Slawomir K. Grzechnik, Hsiu-Ju Chiu, Jie Ouyang, Guenter Wolf, Bill West, Kevin Quijano, Heath E. Klock, Xianhong Wang, Scott A. Lesley, Michael Didonato, Jamison Cambell, Polat Abdubek, Marc-André Elsliger, Jaume M. Canaves, Eric Koesema, Kin Moy, Lukasz Jaroszewski, Frank von Delft, Alyssa Robb, Keith O. Hodgson, Andrew T. Morse, Juli Vincent, Inna Levin, Jeff Velasquez, John Wooley, Cathy Karlak, Mitchell D. Miller, Glen Spraggon, Peter Kuhn, Eric Hampton, Robert Schwarzenbacher, Tanya Biorac, Adam Godzik, Daniel McMullan, Ron Reyes, Timothy M. McPhillips, Eric Sims, Ian A. Wilson, Eileen Ambing, and Ashley M. Deacon

Subjects
chemistry.chemical_classification, Models, Molecular, Binding Sites, Chemistry, Stereochemistry, Resolution (electron density), Molecular Sequence Data, Crystal structure, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, Mice, Structural Biology, Oxidoreductase, Structural Homology, Protein, Animals, Amino Acid Sequence, Quinone Reductases, Oxidoreductases, Molecular Biology, NADP
Published
2004

43. Crystal structure of a PIN (PilT N-terminus) domain (AF0591) from Archaeoglobus fulgidus at 1.90 A resolution

Author

Jie Ouyang, Andreas Kreusch, Rebecca Page, John Wooley, Heath E. Klock, Ashley M. Deacon, Mitchell D. Miller, Hsiu-Ju Chiu, Jaume M. Canaves, Glen Spraggon, Mike DiDonato, Jamison Campbell, Henry van den Bedem, Linda S. Brinen, Guenter Wolf, Kin Moy, Eric Hampton, Marc-André Elsliger, Keith O. Hodgson, Tanya Biorac, Adam Godzik, Ian A. Wilson, Peter Kuhn, Jeff Velasquez, Fred Rezezadeh, Ross Floyd, Bill West, Eileen Ambing, Ron Reyes, Raymond C. Stevens, Timothy M. McPhillips, Frank von Delft, Xiaoping Dai, Eric Sims, John S. Kovarik, Eric Koesema, Robert Schwarzenbacher, Alyssa Robb, Andrew T. Morse, Juli Vincent, Xianhong Wang, Scott A. Lesley, Kevin Quijano, Carina Grittini, Slawomir K. Grzechnik, Polat Abdubek, Daniel McMullan, Inna Levin, Cathy Karlak, Qingping Xu, and Lukasz Jaroszewski

Subjects
Exonucleases, Models, Molecular, Protein Folding, Protein Conformation, Archaeal Proteins, Molecular Sequence Data, Crystal structure, Siphoviridae, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Viral Proteins, Protein structure, Structural Biology, Amino Acid Sequence, Molecular Biology, Peptide sequence, Binding Sites, Sequence Homology, Amino Acid, Resolution (electron density), Archaeoglobus fulgidus, Protein Structure, Tertiary, N-terminus, Crystallography, Protein folding, PIN domain
Published
2004

44. Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution

Author

Glen Spraggon, Slawomir K. Grzechnik, Andreas Kreusch, Rebecca Page, Kevin Quijano, Polat Abdubek, Jie Ouyang, Marc-André Elsliger, H.-J. Chiu, Cathy Karlak, Adam Godzik, Raymond C. Stevens, Alyssa Robb, Said Eshagi, Frank von Delft, Kin Moy, Tanja Biorac, Guenter Wolf, Andrew T. Morse, Juli Vincent, Linda S. Brinen, Heath E. Klock, Jaume M. Canaves, Carina Grittini, Robert Schwarzenbacher, John Wooley, Ashley M. Deacon, Daniel McMullan, Inna Levin, Peter Kuhn, Xiaoping Dai, Jamison Cambell, Ian A. Wilson, Ross Floyd, Eric Koesema, Mitchell D. Miller, Jeff Velasquez, Eileen Ambing, Xianhong Wang, Scott A. Lesley, Keith O. Hodgson, John S. Kovarik, Lukasz Jaroszewski, Mike DiDonato, Henry van den Bedem, Qingping Xu, Eric Hampton, Bill West, and Timothy M. McPhillips

Subjects
Models, Molecular, biology, Chemistry, Resolution (electron density), Molecular Sequence Data, Crystal structure, biology.organism_classification, Crystallography, X-Ray, Biochemistry, Crystallography, Bacterial Proteins, Structural Biology, Thermotoga maritima, Transferase, Amino Acid Sequence, Aspartate Aminotransferases, Molecular Biology, Peptide sequence
Published
2004

46. The first crystal structure of cyclic GMP-dependent protein kinase Iβ dimerization/docking domain reveals molecular details of isoform-specific anchoring

Author

Glen Spraggon, Darren E. Casteel, Eric V. Smith-Nguyen, Susan S. Taylor, Choel Kim, Renate B. Pilz, Banumathi Sankaran, and Eric Hampton

Subjects
Gene isoform, Pharmacology, Cyclic gmp, Docking (molecular), Chemistry, Poster Presentation, Pharmacology toxicology, Biophysics, Anchoring, Pharmacology (medical), Crystal structure, Bioinformatics, Protein kinase A
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