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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Context-dependent protein folding of a virulence peptide in the bacterial and host environments: Structure of an SycH-YopH chaperone-effector complex
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Context-dependent protein folding of a virulence peptide in the bacterial and host environments: Structure of an SycH-YopH chaperone-effector complex

机译：上下文相关的蛋白质折叠的毒性肽在细菌和宿主环境中:结构的SycH-YopH chaperone-effector复杂的

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Yersinia pestis injects numerous bacterial proteins into host cells through an organic nanomachine called the type 3 secretion system. One such substrate is the tyrosine phosphatase YopH, which requires an interaction with a cognate chaperone in order to be effectively injected. Here, the first crystal structure of a SycH-YopH complex is reported, determined to 1.9? resolution. The structure reveals the presence of (i) a nonglobular polypeptide in YopH, (ii) a so-called β-motif in YopH and (iii) a conserved hydrophobic patch in SycH that recognizes the β-motif. Biochemical studies establish that the β-motif is critical to the stability of this complex. Finally, since previous work has shown that the N-terminal portion of YopH adopts a globular fold that is functional in the host cell, aspects of how this polypeptide adopts radically different folds in the host and in the bacterial environments are analysed.
机译：鼠疫杆菌注入大量的细菌通过有机蛋白质进入宿主细胞nanomachine称为3型分泌系统。一个这样的酪氨酸磷酸酶底物YopH,这需要一个交互同源女伴为了有效注入。SycH-YopH复杂的报告,决定1.9 ?决议。(我)YopH nonglobular多肽,(ii)所谓β主题YopH和(iii)守恒的疏水性补丁SycH认识到β主题。β主题的稳定性至关重要复杂。YopH实行的氨基端部分球状折叠功能的主机细胞,该多肽采用的方面完全不同的主机和折叠细菌的环境进行了分析。

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