1JZO

DsbC C101S

1JZO の概要

• エントリーDOI: 10.2210/pdb1jzo/pdb
• 関連するPDBエントリー: 1eej 1JZD
• 分子名称: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC (2 entities in total)
• 機能のキーワード: disulfide bond isomerase, thiol oxidoreductase, dsbc, thioredoxin fold, oxidoreductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P21892
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46943.90

構造登録者

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P. (登録日: 2001-09-17, 公開日: 2003-03-08, 最終更新日: 2024-11-06)

主引用文献

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P.
The Disulfide Bond Isomerase DsbC is Activated by an Immunoglobulin-fold Thiol Oxidoreductase: Crystal Structure of the DsbC-DsbDalpha complex.
Embo J., 21:4774-4784, 2002

PubMed Abstract: The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding. It is specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2.3 A crystal structure of the complex shows for the first time the specific interactions between two thiol oxidoreductases. DsbDalpha is a novel thiol oxidoreductase with the active site cysteines embedded in an immunoglobulin fold. It binds into the central cleft of the V-shaped DsbC dimer, which assumes a closed conformation on complex formation. Comparison of the complex with oxidized DsbDalpha reveals major conformational changes in a cap structure that regulates the accessibility of the DsbDalpha active site. Our results explain how DsbC is selectively activated by DsbD using electrons derived from the cytoplasm.

PubMed: 12234918
DOI: 10.1093/emboj/cdf489

実験手法

X-RAY DIFFRACTION (1.92 Å)