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3 results on '"Sim DW"'

1. C-terminal dimerization of apo-cyclic AMP receptor protein validated in solution.

Author

Sim DW, Choi JW, Kim JH, Ryu KS, Kim M, Yu HW, Jo KS, Kim EH, Seo MD, Jeon YH, Lee BJ, Kim YP, and Won HS

Subjects
Amino Acid Sequence, Apoproteins genetics, Apoproteins metabolism, Circular Dichroism, Cyclic AMP chemistry, Cyclic AMP metabolism, Cyclic AMP Receptor Protein genetics, Cyclic AMP Receptor Protein metabolism, Escherichia coli Proteins genetics, Escherichia coli Proteins metabolism, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Binding, Protein Structure, Secondary, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Apoproteins chemistry, Cyclic AMP Receptor Protein chemistry, Escherichia coli Proteins chemistry, Protein Domains, Protein Multimerization, Solutions chemistry
Abstract

Although cyclic AMP receptor protein (CRP) has long served as a typical example of effector-mediated protein allostery, mechanistic details into its regulation have been controversial due to discrepancy between the known crystal structure and NMR structure of apo-CRP. Here, we report that the recombinant protein corresponding to its C-terminal DNA-binding domain (CDD) forms a dimer. This result, together with structural information obtained in the present NMR study, is consistent with the previous crystal structure and validates its relevance also in solution. Therefore, our findings suggest that dissociation of the CDD may be critically involved in cAMP-induced allosteric activation of CRP., (© 2017 Federation of European Biochemical Societies.)

Published
2017
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2. Structural identification of the lipopolysaccharide-binding capability of a cupin-family protein from Helicobacter pylori.

Author

Sim DW, Kim JH, Kim HY, Jang JH, Lee WC, Kim EH, Park PJ, Lee KH, and Won HS

Subjects
Bacterial Proteins metabolism, Carrier Proteins metabolism, Crystallography, X-Ray, Helicobacter pylori metabolism, Lipopolysaccharides metabolism, Magnetic Resonance Spectroscopy, Protein Binding, Surface Properties, Bacterial Proteins chemistry, Carrier Proteins chemistry, Helicobacter pylori chemistry, Lipopolysaccharides chemistry, Protein Conformation
Abstract

We solved the crystal structure of a functionally uncharacterized protein, HP0902, from Helicobacter pylori. Its structure demonstrated an all-β cupin fold that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. In contrast, isothermal titration calorimetry and NMR titration demonstrated that HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins. This report constitutes the first identification of an LPS-interacting protein, both in the cupin family and in H. pylori. Furthermore, identification of the ability of HP0902 to bind LPS uncovers a putative role for this protein in H. pylori pathogenicity., (© 2016 Federation of European Biochemical Societies.)

Published
2016
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3. Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution.

Author

Lee YS, Ryu KS, Kim SJ, Ko HS, Sim DW, Jeon YH, Kim EH, Choi WS, and Won HS

Subjects
Dimerization, Escherichia coli Proteins genetics, Escherichia coli Proteins metabolism, Heat-Shock Proteins genetics, Heat-Shock Proteins metabolism, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Protein Interaction Domains and Motifs, Protein Structure, Quaternary, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Solutions, Spectrometry, Fluorescence, Escherichia coli Proteins chemistry, Heat-Shock Proteins chemistry
Abstract

Upon dimerization by oxidation, Hsp33 functions as a molecular chaperone in prokaryotes. Previously published structures of both the inactive and active species are of doubtful relevance to the solution conformations since the inactive (reduced) crystal structure was dimeric, while the active (oxidized) species was crystallized with a truncation of its regulation domain. The interdomain contact site of the inactive monomer, identified in this work, is consistent with that previously observed in the reduced dimer crystal. In contrast, fluorescence quenching of the active dimer contradicted the results expected from the domain-swapped fold observed in the truncated dimer crystal. The results of this study provide important new information concerning controversial issues in the activation process of Hsp33., (Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Published
2012
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