2ju5

DsbH OxidoreductaseDsbH Oxidoreductase

Structural highlights 2ju5 is a 1 chain structure with sequence from Chlamydia pneumoniae tw-183. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DSBH_CHLPN] Catalyzes the reduction of disulfide bonds. May function in reducing intermolecular disulfides between proteins and small molecules in the periplasm, or keeping a specific subset of periplasmic proteins reduced, or maintaining the periplasm of Chlamydia in a generally reducing state. Seems to be unable to oxidize thiols into disulfides and does not display disulfide bond isomerase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2ju5, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image