Search

Your search keyword '"Burra, P."' showing total 3 results
Start Over Author "Burra, P." Journal acta crystallographica section f: structural biology communications
3 results on '"Burra, P."'

1. The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 Å resolution reveals a new fold (the ABATE domain) and suggests its possible role as a transcription regulator

Author

Bakolitsa, Constantina, Bateman, Alex, Jin, Kevin K, McMullan, Daniel, Krishna, S Sri, Miller, Mitchell D, Abdubek, Polat, Acosta, Claire, Astakhova, Tamara, Axelrod, Herbert L, Burra, Prasad, Carlton, Dennis, Chiu, Hsiu-Ju, Clayton, Thomas, Das, Debanu, Deller, Marc C, Duan, Lian, Elias, Ylva, Feuerhelm, Julie, Grant, Joanna C, Grzechnik, Anna, Grzechnik, Slawomir K, Han, Gye Won, Jaroszewski, Lukasz, Klock, Heath E, Knuth, Mark W, Kozbial, Piotr, Kumar, Abhinav, Marciano, David, Morse, Andrew T, Murphy, Kevin D, Nigoghossian, Edward, Okach, Linda, Oommachen, Silvya, Paulsen, Jessica, Reyes, Ron, Rife, Christopher L, Sefcovic, Natasha, Tien, Henry, Trame, Christine B, Trout, Christina V, van den Bedem, Henry, Weekes, Dana, White, Aprilfawn, Xu, Qingping, Hodgson, Keith O, Wooley, John, Elsliger, Marc-André, Deacon, Ashley M, Godzik, Adam, Lesley, Scott, and Wilson, Ian A

Subjects
Genetics, Underpinning research, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Aetiology, Generic health relevance, Amino Acid Sequence, Bacterial Proteins, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Tertiary, Rhodobacteraceae, Sequence Alignment, Zinc Fingers, Chemical Sciences, Biological Sciences, Biophysics
Abstract

The crystal structure of Jann_2411 from Jannaschia sp. strain CCS1, a member of the Pfam PF07336 family classified as a domain of unknown function (DUF1470), was solved to a resolution of 1.45 Å by multiple-wavelength anomalous dispersion (MAD). This protein is the first structural representative of the DUF1470 Pfam family. Structural analysis revealed a two-domain organization, with the N-terminal domain presenting a new fold called the ABATE domain that may bind an as yet unknown ligand. The C-terminal domain forms a treble-clef zinc finger that is likely to be involved in DNA binding. Analysis of the Jann_2411 protein and the broader ABATE-domain family suggests a role as stress-induced transcriptional regulators.

Published
2010

2. Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino‐acid metabolism

Author

Bakolitsa, Constantina, Kumar, Abhinav, Jin, Kevin K, McMullan, Daniel, Krishna, S Sri, Miller, Mitchell D, Abdubek, Polat, Acosta, Claire, Astakhova, Tamara, Axelrod, Herbert L, Burra, Prasad, Carlton, Dennis, Chen, Connie, Chiu, Hsiu-Ju, Clayton, Thomas, Das, Debanu, Deller, Marc C, Duan, Lian, Elias, Ylva, Ellrott, Kyle, Ernst, Dustin, Farr, Carol L, Feuerhelm, Julie, Grant, Joanna C, Grzechnik, Anna, Grzechnik, Slawomir K, Han, Gye Won, Jaroszewski, Lukasz, Johnson, Hope A, Klock, Heath E, Knuth, Mark W, Kozbial, Piotr, Marciano, David, Morse, Andrew T, Murphy, Kevin D, Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Paulsen, Jessica, Puckett, Christina, Reyes, Ron, Rife, Christopher L, Sefcovic, Natasha, Tien, Henry J, Trame, Christine B, Trout, Christina V, van den Bedem, Henry, Weekes, Dana, White, Aprilfawn, Xu, Qingping, Hodgson, Keith O, Wooley, John, Elsliger, Marc-Andre, Deacon, Ashley M, Godzik, Adam, Lesley, Scott A, and Wilson, Ian A

Subjects
Biochemistry and Cell Biology, Bioinformatics and Computational Biology, Biological Sciences, Genetics, 2.1 Biological and endogenous factors, Aetiology, Generic health relevance, Amino Acid Sequence, Amino Acids, Bacillus, Bordetella bronchiseptica, Chorismate Mutase, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, Rhodobacteraceae, Structural Homology, Protein, Chemical Sciences, Biophysics, Biological sciences, Chemical sciences
Abstract

The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis.

Published
2010

3. The structure of the first representative of Pfam family PF09836 reveals a two‐domain organization and suggests involvement in transcriptional regulation

Author

Das, Debanu, Grishin, Nick V, Kumar, Abhinav, Carlton, Dennis, Bakolitsa, Constantina, Miller, Mitchell D, Abdubek, Polat, Astakhova, Tamara, Axelrod, Herbert L, Burra, Prasad, Chen, Connie, Chiu, Hsiu-Ju, Chiu, Michelle, Clayton, Thomas, Deller, Marc C, Duan, Lian, Ellrott, Kyle, Ernst, Dustin, Farr, Carol L, Feuerhelm, Julie, Grzechnik, Anna, Grzechnik, Slawomir K, Grant, Joanna C, Han, Gye Won, Jaroszewski, Lukasz, Jin, Kevin K, Johnson, Hope A, Klock, Heath E, Knuth, Mark W, Kozbial, Piotr, Krishna, S Sri, Marciano, David, McMullan, Daniel, Morse, Andrew T, Nigoghossian, Edward, Nopakun, Amanda, Okach, Linda, Oommachen, Silvya, Paulsen, Jessica, Puckett, Christina, Reyes, Ron, Rife, Christopher L, Sefcovic, Natasha, Tien, Henry J, Trame, Christine B, van den Bedem, Henry, Weekes, Dana, Wooten, Tiffany, Xu, Qingping, Hodgson, Keith O, Wooley, John, Elsliger, Marc-André, Deacon, Ashley M, Godzik, Adam, Lesley, Scott A, and Wilson, Ian A

Subjects
Biochemistry and Cell Biology, Biological Sciences, Genetics, Underpinning research, 1.1 Normal biological development and functioning, Amino Acid Sequence, Bacterial Proteins, Crystallography, X-Ray, Gene Expression Regulation, Genome, Bacterial, Models, Molecular, Molecular Sequence Data, Neisseria gonorrhoeae, Protein Structure, Quaternary, Protein Structure, Tertiary, Structural Homology, Protein, Transcription, Genetic, Chemical Sciences, Biophysics, Biological sciences, Chemical sciences
Abstract

Proteins with the DUF2063 domain constitute a new Pfam family, PF09836. The crystal structure of a member of this family, NGO1945 from Neisseria gonorrhoeae, has been determined and reveals that the N-terminal DUF2063 domain is likely to be a DNA-binding domain. In conjunction with the rest of the protein, NGO1945 is likely to be involved in transcriptional regulation, which is consistent with genomic neighborhood analysis. Of the 216 currently known proteins that contain a DUF2063 domain, the most significant sequence homologs of NGO1945 (∼40-99% sequence identity) are from various Neisseria and Haemophilus species. As these are important human pathogens, NGO1945 represents an interesting candidate for further exploration via biochemical studies and possible therapeutic intervention.

Published
2010

Catalog

Books, media, physical & digital resources
See catalog results