1G0T

DSBC MUTANT C101S

1G0T の概要

• エントリーDOI: 10.2210/pdb1g0t/pdb
• 関連するPDBエントリー: 1eej
• 分子名称: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC, DI(HYDROXYETHYL)ETHER (3 entities in total)
• 機能のキーワード: thiol oxidoreductase, protein disulfide bond isomerase, thioredoxin fold, isomerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47050.02

構造登録者

Haebel, P.W.,Metcalf, P. (登録日: 2000-10-09, 公開日: 2003-02-04, 最終更新日: 2024-11-20)

主引用文献

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P.
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
Embo J., 21:4774-4784, 2002

PubMed Abstract: DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.

PubMed: 10700276
DOI: 10.1093/emboj/cdf489

実験手法

X-RAY DIFFRACTION (2.6 Å)