Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex.
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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细菌和宿主环境中毒力肽的上下文依赖性蛋白质折叠：SycH-YopH 分子伴侣效应复合物的结构。
DOI：
10.1107/s0907444912051086
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Stebbins,CErec
中科院分区：
文献类型：
--
作者：
Vujanac,Milos;Stebbins,CErec
鼠疫耶尔森氏菌通过称为 3 型分泌系统的有机纳米机器将大量细菌蛋白注入宿主细胞。其中一种底物是酪氨酸磷酸酶 YopH，它需要与同源伴侣相互作用才能有效注射。在此，报道了 SycH-YopH 复合物的第一个晶体结构，分辨率为 1.9 Å。该结构揭示了 (i) YopH 中存在非球状多肽，(ii) YopH 中存在所谓的 β-基序，以及 (iii) SycH 中识别 β-基序的保守疏水片段。生化研究表明，β-基序对该复合物的稳定性至关重要。最后，由于之前的工作表明 YopH 的 N 端部分采用了在宿主细胞中具有功能的球状折叠，因此分析了该多肽如何在宿主和细菌环境中采用完全不同的折叠。
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 Å 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.