2bho

Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT

spinqualitylabelsall models 2bho, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bho is a 1 chain structure with sequence from "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. Ligands: PT Related: 2bsh, 2bsi, 2bsj Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SYCT_YEREN] Functions as a specific chaperone for YopT. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Several Gram-negative pathogens deploy type III secretion systems (TTSSs) as molecular syringes to inject effector proteins into host cells. Prior to secretion, some of these effectors are accompanied by specific type III secretion chaperones. The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT, a cysteine protease that inactivates the small GTPase RhoA of targeted host cells. We solved the crystal structure of SycT at 2.5 angstroms resolution. Despite limited sequence similarity among TTSS chaperones, the SycT structure revealed a global fold similar to that exhibited by other structurally solved TTSS chaperones. The dimerization domain of SycT, however, differed from that of all other known TTSS chaperone structures. Thus, the dimerization domain of TTSS chaperones does not likely serve as a general recognition pattern for downstream processing of effector/chaperone complexes. Yersinia Yop effectors are bound to their specific Syc chaperones close to the Yop N termini, distinct from their catalytic domains. Here, we showed that the catalytically inactive YopT(C139S) is reduced in its ability to bind SycT, suggesting an ancillary interaction between YopT and SycT. This interaction could maintain the protease inactive prior to secretion or could influence the secretion competence and folding of YopT. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycT.,Locher M, Lehnert B, Krauss K, Heesemann J, Groll M, Wilharm G J Biol Chem. 2005 Sep 2;280(35):31149-55. Epub 2005 Jul 6. PMID:16000312 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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