Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium

Heras, B, Totsika, M, Jarrott, R, Shouldice, SR, Guncar, G, Achard, MES, Wells, TJ, Argente, MP, McEwan, AG and Schembri, MA (2010) Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium. Journal of Biological Chemistry, 285 24: 18423-18432. doi:10.1074/jbc.M110.101360

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Author Heras, B
Totsika, M
Jarrott, R
Shouldice, SR
Guncar, G
Achard, MES
Wells, TJ
Argente, MP
McEwan, AG
Schembri, MA
Title Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium
Formatted title
Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2010-06-11
Sub-type Article (original research)
DOI 10.1074/jbc.M110.101360
Open Access Status File (Publisher version)
Volume 285
Issue 24
Start page 18423
End page 18432
Total pages 10
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2011
Language eng
Subject 0904 Chemical Engineering
0601 Biochemistry and Cell Biology
Formatted 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.
Copyright © 2011 by American Society for Biochemistry and Molecular Biology
Keyword Bacterial toxins
Disulfide
Enzyme mechanisms
Protein folding
Protein structure
Bacterial virulence
Disulfide catalysis
Dsb proteins
Redox homeostasis
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Sun, 27 Jun 2010, 00:05:03 EST