3A5X

L-type straight flagellar filament made of full-length flagellin

3A5X の概要

• エントリーDOI: 10.2210/pdb3a5x/pdb
• EMDBエントリー: 1641
• 分子名称: Flagellin (1 entity in total)
• 機能のキーワード: flagellin, flagellar filament, helical reconstruction, bacterial flagellum, secreted, structural protein, motor protein
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51537.18

構造登録者

Maki-Yonekura, S.,Yonekura, K.,Namba, K. (登録日: 2009-08-13, 公開日: 2010-03-16, 最終更新日: 2024-03-13)

主引用文献

Maki-Yonekura, S.,Yonekura, K.,Namba, K.
Conformational change of flagellin for polymorphic supercoiling of the flagellar filament
Nat.Struct.Mol.Biol., 17:417-422, 2010

PubMed Abstract: 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.

PubMed: 20228803
DOI: 10.1038/nsmb.1774

実験手法

ELECTRON MICROSCOPY (4 Å)