1UC7

Crystal structure of DsbDgamma

1UC7 の概要

• エントリーDOI: 10.2210/pdb1uc7/pdb
• 分子名称: Thiol:disulfide interchange protein dsbD (2 entities in total)
• 機能のキーワード: thioredoxin-fold, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (By similarity): P58162
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27917.44

構造登録者

Kim, J.H.,Kim, S.J.,Jeong, D.G.,Son, J.H.,Ryu, S.E. (登録日: 2003-04-09, 公開日: 2004-04-27, 最終更新日: 2024-10-23)

主引用文献

Kim, J.H.,Kim, S.J.,Jeong, D.G.,Son, J.H.,Ryu, S.E.
Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1)
FEBS LETT., 543:164-169, 2003

PubMed Abstract: The Escherichia coli transmembrane protein DsbD transfers electrons from the cytoplasm to the periplasm through a cascade of thiol-disulfide exchange reactions. In this process, the C-terminal periplasmic domain of DsbD (DsbDgamma) shuttles the reducing potential from the membrane domain (DsbDbeta) to the N-terminal periplasmic domain (DsbDalpha). The crystal structure of DsbDgamma determined at 1.9 A resolution reveals that the domain has a thioredoxin fold with an extended N-terminal stretch. In comparison to thioredoxin, the DsbDgamma structure exhibits the stabilized active site conformation and the extended active site alpha2 helix that explain the domain's substrate specificity and the redox potential shift, respectively. The hypothetical model of the DsbDgamma:DsbDalpha complex based on the DsbDgamma structure and previous structural studies indicates that the conserved hydrophobic residue in the C-X-X-C motif of DsbDgamma may be important in the specific recognition of DsbDalpha.

PubMed: 12753926
DOI: 10.1016/S0014-5793(03)00434-4

実験手法

X-RAY DIFFRACTION (1.9 Å)