2ju5
From Proteopedia
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DsbH Oxidoreductase
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.
About this Structure
2JU5 is a Single protein structure of sequence from Chlamydia pneumoniae. Full crystallographic information is available from OCA.
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:18003611
Page seeded by OCA on Wed Jan 23 10:41:31 2008
