4gf3 | pdb_00004gf3

Structure of a SycH-YopH Chaperone-Effector Complex

spinqualitylabelsall models 4gf3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gf3 is a 2 chain structure with sequence from "bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900 and "bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: sycH, YP_pCD87, YPCD1.95c ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900), yopH, yop51 ("Bacterium enterocoliticum" Schleifstein and Coleman 1939) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [YOPH_YEREN] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages. Publication Abstract from PubMed Yersinia pestis injects numerous bacterial proteins into host cells through an organic nanomachine called the type 3 secretion system. One such substrate is the tyrosine phosphatase YopH, which requires an interaction with a cognate chaperone in order to be effectively injected. Here, the first crystal structure of a SycH-YopH complex is reported, determined to 1.9 A resolution. The structure reveals the presence of (i) a nonglobular polypeptide in YopH, (ii) a so-called beta-motif in YopH and (iii) a conserved hydrophobic patch in SycH that recognizes the beta-motif. Biochemical studies establish that the beta-motif is critical to the stability of this complex. Finally, since previous work has shown that the N-terminal portion of YopH adopts a globular fold that is functional in the host cell, aspects of how this polypeptide adopts radically different folds in the host and in the bacterial environments are analysed. Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex.,Vujanac M, Stebbins CE Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):546-54. doi:, 10.1107/S0907444912051086. Epub 2013 Mar 9. PMID:23519663 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase

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