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Structural and Biochemical Characterization of the Oxidoreductase NmDsbA3 from Neisseria meningitidis
Citation
Vivian, JP and Scoullar, J and Robertson, AL and Bottomley, SP and Horne, HJ and Chin, Y and Wielens, J and Thompson, PE and Velkov, T and Piek, S and Byrnes, E and Beddoe, T and Wilce, MC and Kahler, CM and Rossjohn, J and Scanlon, MJ, Structural and Biochemical Characterization of the Oxidoreductase NmDsbA3 from Neisseria meningitidis, Journal of Biological Chemistry, 283, (47) pp. 32452-32461. ISSN 1083-351X (2008) [Refereed Article]
DOI: doi:10.1074/jbc.M803990200
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.
Item Details
Item Type: | Refereed Article |
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Keywords: | DsbA oxidoreductase specificity structure |
Research Division: | Biological Sciences |
Research Group: | Biochemistry and cell biology |
Research Field: | Structural biology (incl. macromolecular modelling) |
Objective Division: | Expanding Knowledge |
Objective Group: | Expanding knowledge |
Objective Field: | Expanding knowledge in the biological sciences |
UTAS Author: | Horne, HJ (Dr James Horne) |
ID Code: | 53316 |
Year Published: | 2008 |
Web of Science® Times Cited: | 23 |
Deposited By: | Central Science Laboratory |
Deposited On: | 2008-11-25 |
Last Modified: | 2008-11-25 |
Downloads: | 0 |
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