The cryo-EM structure of the bacterial flagellum cap complex suggests a molecular mechanism for filament elongation

The cryo-EM structure of the bacterial flagellum cap complex suggests a molecular mechanism for filament elongation
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细菌鞭毛帽复合物的冷冻电镜结构揭示了细丝伸长的分子机制

DOI:
10.1101/807677
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发表时间:
2019
期刊:
--
影响因子:
--
通讯作者:
Al-Otaibi N
Al-Otaibi N
中科院分区:
--
文献类型:
--
作者:
Al-Otaibi N

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细菌鞭毛是一种非凡的分子马达,其在细菌中的主要功能是通过从细菌细胞伸出的细丝的旋转来促进运动。由蛋白质 FliD 寡聚物组成的帽复合物位于鞭毛尖端,对于细丝组装以及某些细菌表面的粘附至关重要。然而,完整的帽复合物的结构及其与丝相互作用的分子基础仍然难以捉摸。在这里,我们报告了空肠弯曲杆菌复合物的冷冻电镜结构,该结构揭示了 FliD 是五聚体,原聚体的 N 末端区域在多个亚基之间形成了广泛的接触,从而有助于 FliD 寡聚化。我们还证明了nativeC.空肠鞭毛丝是 11 股,与之前发表的冷冻电镜结构相反,并提出了丝帽相互作用的分子模型。
The bacterial flagellum is a remarkable molecular motor, whose primary function in bacteria is to facilitate motility through the rotation of a filament protruding from the bacterial cell. A cap complex, consisting of an oligomer of the protein FliD, is localized at the tip of the flagellum, and is essential for filament assembly, as well as adherence to surfaces in some bacteria. However, the structure of the intact cap complex, and the molecular basis for its interaction with the filament, remains elusive. Here we report the cryo-EM structure of theCampylobacter jejunicap complex, which reveals that FliD is pentameric, with the N-terminal region of the protomer forming an extensive set of contacts across several subunits, that contribute to FliD oligomerization. We also demonstrate that the nativeC. jejuniflagellum filament is 11-stranded, contrary to a previously published cryo-EM structure, and propose a molecular model for the filament-cap interaction.
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