Structure of the Yersinia type III secretory system chaperone SycE

被引:70
作者
Birtalan, S [1 ]
Ghosh, P [1 ]
机构
[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1038/nsb1101-974
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the type III secretory system of bacterial pathogens, a large number of sequence-divergent but characteristically small (similar to 14-19 kDa), acidic (pI similar to4-5) chaperone proteins have been identified. We present the 1.74 Angstrom resolution crystal structure of the Yersinia pseudotuberculosis chaperone SycE, whose action in promoting translocation of YopE into host macrophages is essential to Yersinia pathogenesis. SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components. These patches are formed by structurally key residues that are conserved among many chaperones, suggesting shared structural and functional relationships. A negative electrostatic potential covers almost the entire surface of SycE and is likely conserved in character, but not in detail, among chaperones. The structure provides the first structural insights into possible modes of action of SycE and type III chaperones in general.
引用
收藏
页码:974 / 978
页数:5
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