1K6Z

Crystal Structure of the Yersinia Secretion Chaperone SycE

Summary for 1K6Z

• Entry DOI: 10.2210/pdb1k6z/pdb
• Related: 1G9U 1HUF 1JL5 1JYO 1K3E 1K3S
• Descriptor: Type III secretion chaperone SycE, IMIDAZOLE (3 entities in total)
• Functional Keywords: secretion, chaperone, yersinia pestis, toxin
• Biological source: Yersinia pestis
• Total number of polymer chains: 2
• Total formula weight: 32699.70

Authors

Evdokimov, A.G.,Tropea, J.E.,Routzahn, K.M.,Waugh, D.S. (deposition date: 2001-10-17, release date: 2001-10-31, Last modification date: 2024-11-20)

Primary citation

Evdokimov, A.G.,Tropea, J.E.,Routzahn, K.M.,Waugh, D.S.
Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis.
Acta Crystallogr.,Sect.D, 58:398-406, 2002

PubMed Abstract: 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.

PubMed: 11856824
DOI: 10.1107/S090744490200015X

Experimental method

X-RAY DIFFRACTION (2 Å)