1K6Z

Crystal Structure of the Yersinia Secretion Chaperone SycE

1K6Z の概要

• エントリーDOI: 10.2210/pdb1k6z/pdb
• 関連するPDBエントリー: 1G9U 1HUF 1JL5 1JYO 1K3E 1K3S
• 分子名称: Type III secretion chaperone SycE, IMIDAZOLE (3 entities in total)
• 機能のキーワード: secretion, chaperone, yersinia pestis, toxin
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32699.70

構造登録者

Evdokimov, A.G.,Tropea, J.E.,Routzahn, K.M.,Waugh, D.S. (登録日: 2001-10-17, 公開日: 2001-10-31, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)