9N8H

In situ sheathed flagellar filament of Vibrio cholerae resolved with helical reconstruction.

9N8H の概要

• エントリーDOI: 10.2210/pdb9n8h/pdb
• EMDBエントリー: 49129
• 分子名称: Flagellin D (1 entity in total)
• 機能のキーワード: in situ cryo-em, sheathed flagellar filament, flad vibrio cholerae., motor protein
• 由来する生物種: Vibrio cholerae O1 biovar El Tor str. N16961
• タンパク質・核酸の鎖数: 33
• 化学式量合計: 1318020.26

構造登録者

Wangbiao, G.,Jun, L. (登録日: 2025-02-08, 公開日: 2025-09-24, 最終更新日: 2025-11-12)

主引用文献

Guo, W.,Zhang, S.,Park, J.H.,Stanton, V.,Asp, M.,Herrera, H.,Tai, J.B.,Yue, J.,Wang, J.,Guo, J.,Kumar, R.,Botting, J.M.,Wu, S.,Yan, J.,Klose, K.E.,Yildiz, F.H.,Liu, J.
Structures of the sheathed flagellum reveal mechanisms of assembly and rotation in Vibrio cholerae.
Nat Microbiol, 2025

PubMed Abstract: Motility promotes the complex life cycle and infectious capabilities of Vibrio cholerae and is driven by rotation of a single polar flagellum. The flagellar filament comprises four flagellin proteins (FlaA-D) and is covered by a membranous sheath continuous with the outer membrane. Here we combine in situ cryo-electron microscopy single-particle analysis, fluorescence microscopy and molecular genetics to determine 2.92-3.43 Å structures of the sheathed flagellar filament from intact bacteria. Our data reveal the spatial arrangement of FlaA-D, showing that FlaA localizes at the cell pole and functions as a template for filament assembly involving multiple flagellins. Unlike unsheathed flagellar filaments, the sheathed filament from V. cholerae possesses a highly conserved core but a smooth, hydrophilic surface adjacent to the membranous sheath. A tiny conformational change at the single flagellin level results in a supercoiled filament and curved membranous sheath, supporting a model wherein the filament rotates separately from the sheath, enabling the distinct motility of V. cholerae.

PubMed: 41174224
DOI: 10.1038/s41564-025-02161-x

実験手法

ELECTRON MICROSCOPY (2.73 Å)