4GXZ

Crystal structure of a periplasmic thioredoxin-like protein from Salmonella enterica serovar Typhimurium

4GXZ の概要

• エントリーDOI: 10.2210/pdb4gxz/pdb
• 関連するPDBエントリー: 3L9S 3L9U
• 分子名称: Suppression of copper sensitivity protein (2 entities in total)
• 機能のキーワード: thiol-disulfide oxidoreductase, thioredoxin fold, oxidoreductase, thiol-disulfide oxidation reduction, periplasmic space, isomerase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 84917.32

構造登録者

Shepherd, M.,Heras, B.,King, G.J.,Argente, M.P.,Achard, M.E.S.,King, N.P.,McEwan, A.G.,Schembri, M.A. (登録日: 2012-09-04, 公開日: 2013-07-17, 最終更新日: 2023-11-08)

主引用文献

Shepherd, M.,Heras, B.,Achard, M.E.,King, G.J.,Argente, M.P.,Kurth, F.,Taylor, S.L.,Howard, M.J.,King, N.P.,Schembri, M.A.,McEwan, A.G.
Structural and functional characterization of ScsC, a periplasmic thioredoxin-like protein from Salmonella enterica serovar Typhimurium
Antioxid Redox Signal, 19:1494-1506, 2013

PubMed Abstract: The prototypical protein disulfide bond (Dsb) formation and protein refolding pathways in the bacterial periplasm involving Dsb proteins have been most comprehensively defined in Escherichia coli. However, genomic analysis has revealed several distinct Dsb-like systems in bacteria, including the pathogen Salmonella enterica serovar Typhimurium. This includes the scsABCD locus, which encodes a system that has been shown via genetic analysis to confer copper tolerance, but whose biochemical properties at the protein level are not defined. The aim of this study was to provide functional insights into the soluble ScsC protein through structural, biochemical, and genetic analyses.

PubMed: 23642141
DOI: 10.1089/ars.2012.4939

実験手法

X-RAY DIFFRACTION (2.04 Å)