3CW0

E.coli DmsD

3CW0 の概要

• エントリーDOI: 10.2210/pdb3cw0/pdb
• 分子名称: Twin-arginine leader-binding protein dmsD (2 entities in total)
• 機能のキーワード: dmsd, alpha-helices, chaperone, membrane
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Cell inner membrane ; Peripheral membrane protein : P69853
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 94887.46

構造登録者

Ramasamy, S.,Clemons, W. (登録日: 2008-04-21, 公開日: 2009-04-28, 最終更新日: 2024-02-21)

主引用文献

Ramasamy, S.K.,Clemons, W.M.
Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli.
Acta Crystallogr.,Sect.F, 65:746-750, 2009

PubMed Abstract: The translocation of folded proteins via the twin-arginine translocation (Tat) pathway is regulated to prevent the futile export of inactive substrate. DmsD is part of a class of cytoplasmic chaperones that play a role in preventing certain redox proteins from premature transport. DmsD from Escherichia coli has been crystallized in space group P4(1)2(1)2, with unit-cell parameters a = b = 97.45, c = 210.04 A, in the presence of a small peptide. The structure has been solved by molecular replacement to a resolution of 2.4 A and refined to an R factor of 19.4%. There are four molecules in the asymmetric unit that may mimic a higher order structure in vivo. There appears to be density for the peptide in a predicted binding pocket, which lends support to its role as the signal-recognition surface for this class of proteins.

PubMed: 19652330
DOI: 10.1107/S1744309109023811

実験手法

X-RAY DIFFRACTION (2.4 Å)