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
复制标题
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
中科院分区:
文献类型:
--
作者:
Al-Otaibi N
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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影响因子:
5.6
作者:
Maki, S;Vonderviszt, F;Namba, K
通讯作者:
Namba, K
影响因子:
--
作者:
Imada, Katsumi
通讯作者:
Imada, Katsumi
影响因子:
1.6
作者:
Studier, FW
通讯作者:
Studier, FW
DOI:
10.1016/j.str.2013.08.005
发表时间:
2013-10-08
期刊:
Structure (London, England : 1993)
影响因子:
--
作者:
Song Y;DiMaio F;Wang RY;Kim D;Miles C;Brunette T;Thompson J;Baker D
通讯作者:
Baker D
DOI:
10.2142/biophysics.11.93
发表时间:
2015
期刊:
Biophysics (Nagoya-shi, Japan)
影响因子:
--
作者:
Motojima F
通讯作者:
Motojima F