X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli
X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli
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DOI：
10.1126/science.285.5430.1061
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发表时间：
1999-08-13
期刊：
影响因子：
56.9
通讯作者：
Knight, SD
中科院分区：
文献类型：
--
作者：
Choudhury, D;Thompson, A;Knight, SD
1 型菌毛粘附纤维在肠杆菌科大多数成员中表达，通过 FimH 粘附素介导与宿主细胞上的甘露糖受体的结合。菌毛生物发生通过伴侣/引座途径进行。来自尿路致病性大肠杆菌的 FimC-FimH 分子伴侣-粘附素复合物的 X 射线结构在 2.5 埃分辨率下揭示了碳水化合物识别和菌毛组装的基础。 FimH 的羧基末端菌毛蛋白结构域具有类似免疫球蛋白的折叠，但第七条链缺失，导致部分疏水核心暴露。供体链互补机制（其中伴侣蛋白捐赠一条链来完成菌毛蛋白结构域）解释了伴侣蛋白功能和菌毛生物发生的基础。
Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.