Structural highlights
3l9u is a 1 chain structure with sequence from Salts. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 3c7m, 3a3t, 3f4r, 3bci, 1fvk, 1dsb, 3l9s, 3l9v |
| Gene: | dsbL, STM3193 (SALTS) |
| Activity: | Protein disulfide-isomerase, with EC number 5.3.4.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[A0A0H3NG38_SALTS] Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.[HAMAP-Rule:MF_00932]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium.,Heras B, Totsika M, Jarrott R, Shouldice SR, Guncar G, Achard ME, Wells TJ, Argente MP, McEwan AG, Schembri MA J Biol Chem. 2010 Jun 11;285(24):18423-32. Epub 2010 Mar 16. PMID:20233716[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heras B, Totsika M, Jarrott R, Shouldice SR, Guncar G, Achard ME, Wells TJ, Argente MP, McEwan AG, Schembri MA. Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium. J Biol Chem. 2010 Jun 11;285(24):18423-32. Epub 2010 Mar 16. PMID:20233716 doi:10.1074/jbc.M110.101360
