4GXZ

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

Summary for 4GXZ

• Entry DOI: 10.2210/pdb4gxz/pdb
• Related: 3L9S 3L9U
• Descriptor: Suppression of copper sensitivity protein (2 entities in total)
• Functional Keywords: thiol-disulfide oxidoreductase, thioredoxin fold, oxidoreductase, thiol-disulfide oxidation reduction, periplasmic space, isomerase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 4
• Total formula weight: 84917.32

Authors

Shepherd, M.,Heras, B.,King, G.J.,Argente, M.P.,Achard, M.E.S.,King, N.P.,McEwan, A.G.,Schembri, M.A. (deposition date: 2012-09-04, release date: 2013-07-17, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.04 Å)