1k6z
From Proteopedia
Crystal Structure of the Yersinia Secretion Chaperone SycE
Overview
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.
About this Structure
1K6Z is a Single protein structure of sequence from Yersinia pestis. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 22:23:02 2008
