期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 4, 页码 417-U50出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1774
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资金
- W.M. Keck Advanced Microscopy Laboratory at the University of California, San Francisco
- Ministry of Education, Science and Culture of Japan [16087207]
- Grants-in-Aid for Scientific Research [16087207] Funding Source: KAKEN
The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left-and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.
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