1VRS

Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD

「1SE1」から置き換えられました

1VRS の概要

• エントリーDOI: 10.2210/pdb1vrs/pdb
• 分子名称: Thiol:disulfide interchange protein dsbD (3 entities in total)
• 機能のキーワード: dsbd, immunoglobulin-like, thioredoxin-like, disulfide-linked, oxidoreductase
• 由来する生物種: Escherichia coli str. K12 substr.; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P36655 P36655
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 93193.49

構造登録者

Rozhkova, A.,Stirnimann, C.U.,Frei, P.,Grauschopf, U.,Brunisholz, R.,Gruetter, M.G.,Capitani, G.,Glockshuber, R. (登録日: 2005-06-17, 公開日: 2005-07-12, 最終更新日: 2024-11-20)

主引用文献

Rozhkova, A.,Stirnimann, C.U.,Frei, P.,Grauschopf, U.,Brunisholz, R.,Gruetter, M.G.,Capitani, G.,Glockshuber, R.
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD
Embo J., 23:1709-1719, 2004

PubMed Abstract: DsbD from Escherichia coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC. DsbD contains two periplasmically oriented domains at the N- and C-terminus (nDsbD and cDsbD) that are connected by a central transmembrane (TM) domain. Each domain contains a pair of cysteines that are essential for catalysis. Here, we show that Cys109 and Cys461 form a transient interdomain disulfide bond between nDsbD and cDsbD in the reaction cycle of DsbD. We solved the crystal structure of this catalytic intermediate at 2.85 A resolution, which revealed large relative domain movements in DsbD as a consequence of a strong overlap between the surface areas of nDsbD that interact with DsbC and cDsbD. In addition, we have measured the kinetics of all functional and nonfunctional disulfide exchange reactions between redox-active, periplasmic proteins and protein domains from the oxidative DsbA/B and the reductive DsbC/D pathway. We show that both pathways are separated by large kinetic barriers for nonfunctional disulfide exchange between components from different pathways.

PubMed: 15057279
DOI: 10.1038/sj.emboj.7600178

実験手法

X-RAY DIFFRACTION (2.85 Å)