2ju5: Difference between revisions

Revision as of 19:05, 21 February 2008

DsbH Oxidoreductase

OverviewOverview

The Chlamydia family of human pathogens uses outer envelope proteins that are highly cross-linked by disulfide bonds but nevertheless keeps an unusually high number of unpaired cysteines in its secreted proteins. To gain insight into chlamydial disulfide bond catalysis, the structure, function, and substrate interaction of a novel periplasmic oxidoreductase, termed DsbH, were determined. The structure of DsbH, its redox potential of -269 mV, and its functional properties are similar to thioredoxin and the C-terminal domain of DsbD, i.e. characteristic of a disulfide reductase. As compared with these proteins, the two central residues of the DsbH catalytic motif (CMWC) shield the catalytic disulfide bond and are selectively perturbed by a peptide ligand. This shows that these oxidoreductase family characteristic residues are not only important in determining the redox potential of the catalytic disulfide bond but also in influencing substrate interactions. For DsbH, three functional roles are conceivable; that is, reducing intermolecular disulfides between proteins and small molecules, keeping a specific subset of exported proteins reduced, or maintaining the periplasm of Chlamydia in a generally reducing state.

About this StructureAbout this Structure

2JU5 is a Single protein structure of sequence from Chlamydia pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase., Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS, J Biol Chem. 2008 Jan 11;283(2):824-32. Epub 2007 Nov 14. PMID:18003611

Page seeded by OCA on Thu Feb 21 18:05:53 2008

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OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-The Chlamydia family of human pathogens uses outer envelope proteins that, are highly cross-linked by disulfide bonds, but nevertheless keeps an, unusually high number of unpaired cysteines in its secreted proteins. To, gain insight into chlamydial disulfide bond catalysis, the structure, function, and substrate interaction of a novel periplasmic oxidoreductase, termed DsbH, were determined. The structure of DsbH, its redox potential, of -269 mV, and its functional properties are similar to thioredoxin and, the C-terminal domain of DsbD; i.e., characteristic of a disulfide, reductase. As compared to these proteins, the two central residues of, DsbH's catalytic motif (CMWC) shield the catalytic disulfide bond and are, selectively perturbed by a peptide ligand. This shows that these, oxidoreductase family-characteristic residues are not only important in, determining the redox potential of the catalytic disulfide bond, but also, in influencing substrate interactions. For DsbH three functional roles are, conceivable: reducing intermolecular disulfides between proteins and small, molecules, keeping a specific subset of exported proteins reduced, or, maintaining the periplasm of Chlamyida in a generally reducing state.
+The Chlamydia family of human pathogens uses outer envelope proteins that are highly cross-linked by disulfide bonds but nevertheless keeps an unusually high number of unpaired cysteines in its secreted proteins. To gain insight into chlamydial disulfide bond catalysis, the structure, function, and substrate interaction of a novel periplasmic oxidoreductase, termed DsbH, were determined. The structure of DsbH, its redox potential of -269 mV, and its functional properties are similar to thioredoxin and the C-terminal domain of DsbD, i.e. characteristic of a disulfide reductase. As compared with these proteins, the two central residues of the DsbH catalytic motif (CMWC) shield the catalytic disulfide bond and are selectively perturbed by a peptide ligand. This shows that these oxidoreductase family characteristic residues are not only important in determining the redox potential of the catalytic disulfide bond but also in influencing substrate interactions. For DsbH, three functional roles are conceivable; that is, reducing intermolecular disulfides between proteins and small molecules, keeping a specific subset of exported proteins reduced, or maintaining the periplasm of Chlamydia in a generally reducing state.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH - a novel oxidoreductase., Mac TT, Hacht AV, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS, J Biol Chem. 2007 Nov 14;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18003611 18003611]
+Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase., Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS, J Biol Chem. 2008 Jan 11;283(2):824-32. Epub 2007 Nov 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18003611 18003611]
 [[Category: Chlamydia pneumoniae]]
 [[Category: Single protein]]
-[[Category: Ulmer, T.S.]]
+[[Category: Ulmer, T S.]]
 [[Category: oxidoreductase]]
 [[Category: protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:41:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:05:53 2008''