7CGO

Cryo-EM structure of the flagellar motor-hook complex from Salmonella

これはPDB形式変換不可エントリーです。

7CGO の概要

• エントリーDOI: 10.2210/pdb7cgo/pdb
• EMDBエントリー: 30359
• 分子名称: Flagellar basal-body rod protein FlgG, Flagellar biosynthetic protein FliQ, Flagellar biosynthetic protein FliP, ... (16 entities in total)
• 機能のキーワード: flagella, hook-basal body, motor protein
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720); 詳細
• タンパク質・核酸の鎖数: 219
• 化学式量合計: 7785661.44

構造登録者

Tan, J.X.,Chang, S.H.,Wang, X.F.,Xu, C.H.,Zhou, Y.,Zhang, X.,Zhu, Y.Q. (登録日: 2020-07-01, 公開日: 2021-04-28, 最終更新日: 2025-04-09)

主引用文献

Tan, J.,Zhang, X.,Wang, X.,Xu, C.,Chang, S.,Wu, H.,Wang, T.,Liang, H.,Gao, H.,Zhou, Y.,Zhu, Y.
Structural basis of assembly and torque transmission of the bacterial flagellar motor.
Cell, 184:2665-2679.e19, 2021

PubMed Abstract: The bacterial flagellar motor is a supramolecular protein machine that drives rotation of the flagellum for motility, which is essential for bacterial survival in different environments and a key determinant of pathogenicity. The detailed structure of the flagellar motor remains unknown. Here we present an atomic-resolution cryoelectron microscopy (cryo-EM) structure of the bacterial flagellar motor complexed with the hook, consisting of 175 subunits with a molecular mass of approximately 6.3 MDa. The structure reveals that 10 peptides protruding from the MS ring with the FlgB and FliE subunits mediate torque transmission from the MS ring to the rod and overcome the symmetry mismatch between the rotational and helical structures in the motor. The LP ring contacts the distal rod and applies electrostatic forces to support its rotation and torque transmission to the hook. This work provides detailed molecular insights into the structure, assembly, and torque transmission mechanisms of the flagellar motor.

PubMed: 33882274
DOI: 10.1016/j.cell.2021.03.057

実験手法

ELECTRON MICROSCOPY (3.9 Å)