Torque transmission mechanism of the curved bacterial flagellar hook revealed by cryo-EM.
Torque transmission mechanism of the curved bacterial flagellar hook revealed by cryo-EM.
复制标题
冷冻电镜揭示弯曲细菌鞭毛钩的扭矩传递机制。
DOI:
10.1038/s41594-019-0301-3
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发表时间:
2019
影响因子:
16.8
通讯作者:
Wolf M
中科院分区:
文献类型:
--
作者:
Shibata S;Matsunami H;Aizawa SI;Wolf M
Bacterial locomotion by rotating flagella is achieved through the hook, which transmits torque from the motor to the filament. The hook is a tubular structure composed of a single type of protein, yet it adopts a curved shape. To perform its function, it must be simultaneously flexible and torsionally rigid. The molecular mechanism by which chemically identical subunits form such a dynamic structure is unknown. Here, we show the complete structure of the hook fromSalmonella entericain its supercoiled ‘curved’ state, at 2.9 Å resolution. Subunits in the curved hook are grouped into 11 distinctive conformations, each shared along 11 protofilaments. The domains of the elongated hook subunit behave as rigid bodies connected by two hinge regions. The reconstituted model demonstrates how identical subunits can dynamically change conformation by physical interactions while bending. These multiple subunit states contradict the two-state model, which is a key feature of flagellar polymorphism.