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Structural and biochemical characterisation 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 characterisation of the oxidoreductase NmDsbA3 from Neisseria meningitidis, Journal of biological chemistry, vol. 283, no. 47, pp. 32452-32461, doi: 10.1074/jbc.M803990200.

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Title Structural and biochemical characterisation of the oxidoreductase NmDsbA3 from Neisseria meningitidis
Formatted title Structural and biochemical characterisation of the oxidoreductase NmDsbA3 from Neisseria meningitidis
Author(s) 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.
Journal name Journal of biological chemistry
Volume number 283
Issue number 47
Start page 32452
End page 32461
Publisher American Society of Biological Chemists
Place of publication Baltimore, Md.
Publication date 2008-11-21
ISSN 0021-9258
1083-351X
Summary DsbA is an enzyme found in the periplasm of Gram-negative bacteria that catalyses the formation of disulfide bonds in a diverse array of protein substrates, many of which are involved in bacterial pathogenesis. Whilst 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, whilst 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 reoxidised 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.
Language eng
DOI 10.1074/jbc.M803990200
Field of Research 039999 Chemical Sciences not elsewhere classified
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
HERDC collection year 2008
Copyright notice ©2008, The American Society for Biochemistry and Molecular Biology
Persistent URL http://hdl.handle.net/10536/DRO/DU:30018679

Document type: Journal Article
Collection: School of Medicine
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Created: Fri, 11 Sep 2009, 09:48:02 EST by Rachael Wilson

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