4dvc | pdb_00004dvc

Structural and functional studies of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera toxin production

spinqualitylabelsall models 4dvc, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4dvc is a 1 chain structure with sequence from Vibch. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DMS, SO4 Gene: tpcG (VIBCH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DSBA_VIBCH] Involved in disulfide-bond formation. Required for the functional maturation of secreted virulence factors. Acts by transferring its disulfide bond to other proteins. Publication Abstract from PubMed 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 A resolution crystal structure of TcpG is reported using a cryocooled crystal. This structure is compared with a previous crystal structure determined at 2.1 A 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 beta5-alpha7 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. The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production.,Walden PM, Heras B, Chen KE, Halili MA, Rimmer K, Sharma P, Scanlon MJ, Martin JL Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1290-302. Epub 2012 Sep, 13. PMID:22993083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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