Structure and biogenesis of the capsular F1 antigen from Yersinia pestis:: Preserved folding energy drives fiber formation
Structure and biogenesis of the capsular F1 antigen from Yersinia pestis:: Preserved folding energy drives fiber formation
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DOI：
10.1016/s0092-8674(03)00351-9
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发表时间：
2003-05-30
期刊：
影响因子：
64.5
通讯作者：
Knight, SD
中科院分区：
文献类型：
--
作者：
Zavialov, AV;Berglund, J;Knight, SD
大多数革兰氏阴性病原体表达纤维粘附毒力细胞器，介导针对感染部位的靶向。来自鼠疫病原体鼠疫耶尔森氏菌的 F1 荚膜抗原由单个亚基 (Caf1) 的线性纤维组成，并作为通过伴侣/引座途径组装的非菌毛细胞器的原型。遗传数据与对应于组装过程快照的高分辨率 X 射线结构揭示了纤维形成的结构基础。分子伴侣结合的 Caf1 亚基与纤维中的亚基的比较揭示了一种涉及蛋白质整个疏水核心的新型构象变化。观察到的构象变化表明伴侣捕获了 Caf1 的高能折叠中间体。提出了一种模型，其中子单元的释放可以完成折叠，从而驱动纤维形成。
Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.