1k6z

Crystal Structure of the Yersinia Secretion Chaperone SycE

spinqualitylabelsall models 1k6z, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k6z is a 2 chain structure with sequence from Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: IMD, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YERA_YERPE Positive regulator of YopE. 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 Many bacterial pathogens utilize a type III (contact-dependent) secretion system to inject cytotoxic effector proteins directly into host cells. This ingenious mechanism, designed for both bacterial offense and defense, has been studied most extensively in Yersinia spp. To be exported efficiently, at least three of the effectors (YopE, YopH and YopT) and several other proteins that transit the type III secretion pathway in Yersinia (YopN, YopD and YopB) must first form transient complexes with cognate-specific Yop chaperone (Syc) proteins. The cytotoxic effector YopE, a selective activator of mammalian Rho-family GTPases, associates with SycE. Here, the structure of Y. pestis SycE at 1.95A resolution is reported. SycE possesses a novel fold with an unusual dimerization motif and an intriguing basic cavity located on the dyad axis of the dimer that may participate in its interaction with YopE. Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis.,Evdokimov AG, Tropea JE, Routzahn KM, Waugh DS Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):398-406. Epub 2002, Feb 21. PMID:11856824 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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