3L9V
Crystal Structure of Salmonella enterica serovar Typhimurium SrgA
Summary for 3L9V
| Entry DOI | 10.2210/pdb3l9v/pdb |
| Related | 1DSB 1FVK 3A3T 3BCI 3F4R 3H93 3L9S 3L9U |
| Descriptor | Putative thiol-disulfide isomerase or thioredoxin, 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL, O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | thioredoxin-fold, srga, thiol-disulfide oxidoreductase, isomerase, oxidoreductase |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 5 |
| Total formula weight | 108703.69 |
| Authors | Heras, B.,Jarrott, R.,Shouldice, S.R.,Guncar, G. (deposition date: 2010-01-05, release date: 2010-03-09, Last modification date: 2024-10-16) |
| Primary citation | Heras, B.,Totsika, M.,Jarrott, R.,Shouldice, S.R.,Guncar, G.,Achard, M.E.S.,Wells, T.J.,Argente, M.P.,McEwan, A.G.,Schembri, M.A. Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium J.Biol.Chem., 285:18423-18432, 2010 Cited by PubMed Abstract: In prototypic Escherichia coli K-12 the introduction of disulfide bonds into folding proteins is mediated by the Dsb family of enzymes, primarily through the actions of the highly oxidizing protein EcDsbA. Homologues of the Dsb catalysts are found in most bacteria. Interestingly, pathogens have developed distinct Dsb machineries that play a pivotal role in the biogenesis of virulence factors, hence contributing to their pathogenicity. Salmonella enterica serovar (sv.) Typhimurium encodes an extended number of sulfhydryl oxidases, namely SeDsbA, SeDsbL, and SeSrgA. Here we report a comprehensive analysis of the sv. Typhimurium thiol oxidative system through the structural and functional characterization of the three Salmonella DsbA paralogues. The three proteins share low sequence identity, which results in several unique three-dimensional characteristics, principally in areas involved in substrate binding and disulfide catalysis. Furthermore, the Salmonella DsbA-like proteins also have different redox properties. Whereas functional characterization revealed some degree of redundancy, the properties of SeDsbA, SeDsbL, and SeSrgA and their expression pattern in sv. Typhimurium indicate a diverse role for these enzymes in virulence. PubMed: 20233716DOI: 10.1074/jbc.M110.101360 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.151 Å) |
Structure validation
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