2JU5
DsbH Oxidoreductase
2JU5 の概要
| エントリーDOI | 10.2210/pdb2ju5/pdb |
| NMR情報 | BMRB: 15431 |
| 分子名称 | Thioredoxin Disulfide Isomerase (1 entity in total) |
| 機能のキーワード | protein, oxidoreductase |
| 由来する生物種 | Chlamydophila pneumoniae |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 17671.03 |
| 構造登録者 | |
| 主引用文献 | Mac, T.T.,von Hacht, A.,Hung, K.C.,Dutton, R.J.,Boyd, D.,Bardwell, J.C.,Ulmer, T.S. Insight into Disulfide Bond Catalysis in Chlamydia from the Structure and Function of DsbH, a Novel Oxidoreductase. J.Biol.Chem., 283:824-832, 2008 Cited by PubMed Abstract: 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. PubMed: 18003611DOI: 10.1074/jbc.M707863200 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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