Structural and biochemical characterization of the oxidoreductase NmDsbA3 from neisseria meningitidis

Vivian, Julian P., Scoullar, Jessica, Robertson, Amy L., Bottomley, Stephen P., Horne, James, Chin, Yanni, Wielens, Jerome, Thompson, Philip E., Velkov, Tony, Piek, Susannah, Byres, Emma, Beddoe, Travis, Wilce, Matthew C. J., Kahler, Charlene M., Rossjohn, Jamie and Scanlon, Martin J. (2008) Structural and biochemical characterization of the oxidoreductase NmDsbA3 from neisseria meningitidis. Journal of Biological Chemistry, 283 47: 32452-32461. doi:10.1074/jbc.M803990200

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Author Vivian, Julian P.
Scoullar, Jessica
Robertson, Amy L.
Bottomley, Stephen P.
Horne, James
Chin, Yanni
Wielens, Jerome
Thompson, Philip E.
Velkov, Tony
Piek, Susannah
Byres, Emma
Beddoe, Travis
Wilce, Matthew C. J.
Kahler, Charlene M.
Rossjohn, Jamie
Scanlon, Martin J.
Title Structural and biochemical characterization of the oxidoreductase NmDsbA3 from neisseria meningitidis
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2008-11
Sub-type Article (original research)
DOI 10.1074/jbc.M803990200
Open Access Status File (Publisher version)
Volume 283
Issue 47
Start page 32452
End page 32461
Total pages 10
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Abstract DsbA is an enzyme found in the periplasm of Gram-negative bacteria that catalyzes the formation of disulfide bonds in a diverse array of protein substrates, many of which are involved in bacterial pathogenesis. Although most bacteria possess only a single essential DsbA, Neisseria meningitidis is unusual in that it possesses three DsbAs, although the reason for this additional redundancy is unclear. Two of these N. meningitidis enzymes (NmDsbA1 and NmDsbA2) play an important role in meningococcal attachment to human epithelial cells, whereas NmDsbA3 is considered to have a narrow substrate repertoire. To begin to address the role of DsbAs in the pathogenesis of N. meningitidis, we have determined the structure of NmDsbA3 to 2.3-Å resolution. Although the sequence identity between NmDsbA3 and other DsbAs is low, the NmDsbA3 structure adopted a DsbA-like fold. Consistent with this finding, we demonstrated that NmDsbA3 acts as a thiol-disulfide oxidoreductase in vitro and is reoxidized by Escherichia coli DsbB (EcDsbB). However, pronounced differences in the structures between DsbA3 and EcDsbA, which are clustered around the active site of the enzyme, suggested a structural basis for the unusual substrate specificity that is observed for NmDsbA3.
Keyword Disulfide Bond Formation
Staphylococcus-Aureus Dsba
Escherichia-Coli Dsba
Formation In-Vivo
Destabilizing Disulfide
Formation Invivo
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 17 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 16 Aug 2012, 10:19:53 EST by Susan Allen on behalf of Institute for Molecular Bioscience