3EFP

Crystal structure of the Escherichia coli twin arginine leader peptide binding protein DmsD in a monomeric form

3EFP の概要

• エントリーDOI: 10.2210/pdb3efp/pdb
• 分子名称: Twin-arginine leader-binding protein dmsD, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: twin-arginine translocation (tat), protein targeting, protein translocation, chaperone, leader peptide, signal peptide, redox enzyme maturation protein (remp)
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein: P69853
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48978.95

構造登録者

Stevens, C.M.,Paetzel, M. (登録日: 2008-09-09, 公開日: 2009-04-07, 最終更新日: 2023-08-30)

主引用文献

Stevens, C.M.,Winstone, T.M.,Turner, R.J.,Paetzel, M.
Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD.
J.Mol.Biol., 389:124-133, 2009

PubMed Abstract: The redox enzyme maturation proteins play an essential role in the proofreading and membrane targeting of protein substrates to the twin-arginine translocase. Functionally, the most thoroughly characterized redox enzyme maturation protein to date is Escherichia coli DmsD (EcDmsD). Herein, we present the X-ray crystal structure of the monomeric form of the EcDmsD refined to 2.0 A resolution, with clear electron density present for each of its 204 amino acid residues. The structural data presented here complement the biochemical data previously generated regarding the function of these twin-arginine translocase leader peptide binding chaperone proteins. Docking and molecular dynamics simulation experiments were used to provide a proposed model for how this chaperone is able to recognize the leader peptide of its substrate DmsA. The interactions observed in the model are in agreement with previous biochemical data and suggest intimate interactions between the conserved twin-arginine motif of the leader peptide of E. coli DmsA and the most conserved regions on the surface of EcDmsD.

PubMed: 19361518
DOI: 10.1016/j.jmb.2009.03.069

実験手法

X-RAY DIFFRACTION (2.01 Å)