Molecular structure of the intact bacterial flagellar basal body.

Molecular structure of the intact bacterial flagellar basal body.
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DOI:
10.1038/s41564-021-00895-y
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发表时间:
2021-06
影响因子:
28.3
通讯作者:
Lea SM
Lea SM
中科院分区:
生物学1区
文献类型:
--
作者:
Johnson S;Furlong EJ;Deme JC;Nord AL;Caesar JJE;Chevance FFV;Berry RM;Hughes KT;Lea SM

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细菌鞭毛是一种大分子蛋白质复合物,使许多物种的运动。细菌鞭毛自组装成一个强大的多组件驱动轴,该驱动轴将内膜中的旋转耦合到微米长的鞭毛细丝,该鞭毛细丝为细菌在粘性流体中游动提供动力。在这里,我们提出了完整的沙门氏菌鞭毛基体的结构,包括内膜转子,驱动轴,和外膜衬套,解决使用冷冻电子显微镜之间的分辨率为2.2和3.7毫米。这些结构揭示了13种不同类型的173个蛋白质分子如何组装成跨越两个膜和一个细胞壁的复合物的分子细节。一端的螺旋驱动轴与转子组件错综复杂地交织在一起,出口门复合体和近端杆与MS环形成相互作用。在另一端,驱动轴远端杆穿过LP-环衬套复合体,其通过与脂多糖的相互作用作为锚定在外膜中的分子轴承。覆盖驱动轴的蛋白质复合物的原位结构提供了对该分子机器的组装过程的分子洞察。
The bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multi-component drive shaft which couples rotation in the inner membrane to the microns-long flagellar filament that powers bacterial swimming in viscous fluids. We here present structures of the intact Salmonella flagellar basal body, encompassing the inner membrane rotor, drive shaft, and outer membrane bushing, solved using cryo-electron microscopy to resolutions between 2.2 and 3.7 Å. The structures reveal molecular details of how 173 protein molecules of 13 different types assemble into a complex spanning two membranes and a cell wall. The helical drive shaft at one end is intricately interwoven with the rotor component with both the export gate complex and the proximal rod forming interactions with the MS-ring. At the other end, the drive shaft distal rod passes through the LP-ring bushing complex, which functions as a molecular bearing anchored in the outer membrane via interactions with the lipopolysaccharide. The in situ structure of a protein complex capping the drive shaft provides molecular insight into the assembly process of this molecular machine.
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影响因子: 9.8
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期刊: Acta crystallographica. Section D, Structural biology
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