The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production

Walden, Patricia M., Heras, Begona, Chen, Kai-En, Halili, Maria A., Rimmer, Kieran, Sharma, Pooja, Scanlon, Martin J. and Martin, Jennifer L. (2012) The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production. Acta Crystallographica Section D-Biological Crystallography, 68 10: 1290-1302.

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Author Walden, Patricia M.
Heras, Begona
Chen, Kai-En
Halili, Maria A.
Rimmer, Kieran
Sharma, Pooja
Scanlon, Martin J.
Martin, Jennifer L.
Title The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production
Journal name Acta Crystallographica Section D-Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
1399-0047
Publication date 2012-10
Sub-type Article (original research)
DOI 10.1107/S0907444912026388
Volume 68
Issue 10
Start page 1290
End page 1302
Total pages 13
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell Publishing
Collection year 2013
Language eng
Abstract The enzyme TcpG is a periplasmic protein produced by the Gram-negative pathogen Vibrio cholerae. TcpG is essential for the production of ToxR-regulated proteins, including virulence-factor pilus proteins and cholera toxin, and is therefore a target for the development of a new class of anti-virulence drugs. Here, the 1.2 Å resolution crystal structure of TcpG is reported using a cryocooled crystal. This structure is compared with a previous crystal structure determined at 2.1 Å resolution from data measured at room temperature. The new crystal structure is the first DsbA crystal structure to be solved at a sufficiently high resolution to allow the inclusion of refined H atoms in the model. The redox properties of TcpG are also reported, allowing comparison of its oxidoreductase activity with those of other DSB proteins. One of the defining features of the Escherichia coli DsbA enzyme is its destabilizing disulfide, and this is also present in TcpG. The data presented here provide new insights into the structure and redox properties of this enzyme, showing that the binding mode identified between E. coli DsbB and DsbA is likely to be conserved in TcpG and that the [beta]5-[alpha]7 loop near the proposed DsbB binding site is flexible, and suggesting that the tense oxidized conformation of TcpG may be the consequence of a short contact at the active site that is induced by disulfide formation and is relieved by reduction.
Keyword Oxidoreductases
High resolution
Virulence
DsbA
Protein-protein interactions
Open Access Mandate Compliance Yes - Open Access (Publisher PDF in repository)
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
Institute for Molecular Bioscience - Publications
 
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