Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy

被引：567

作者：

Yonekura, K

Maki-Yonekura, S

Namba, K ^{[1
]}

机构：

[1] ERATO, JST, Proton NanoMachine Project, Tokyo, Japan

[2] Osaka Univ, Grad Sch Frontier Biosci, Suita, Osaka 565, Japan

[3] ICORP, JST, Dynam NanoMachine Project, Kyoto 6190237, Japan

来源：

NATURE | 2003年 / 424卷 / 6949期

关键词：

D O I：

10.1038/nature01830

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The bacterial flagellar filament is a helical propeller for bacterial locomotion. It is a helical assembly of a single protein, flagellin, and its tubular structure is formed by 11 protofilaments in two distinct conformations, L- and R- type, for supercoiling. The X-ray crystal structure of a flagellin fragment lacking about 100 terminal residues revealed the protofilament structure, but the full filament structure is still essential for understanding the mechanism of supercoiling and polymerization. Here we report a complete atomic model of the R-type filament by electron cryomicroscopy. A density map obtained from image data up to 4Angstrom resolution shows the feature of alpha-helical backbone and some large side chains. The atomic model built on the map reveals intricate molecular packing and an alpha-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament.

引用

页码：643 / 650

页数：8

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