8UMD

Cryo-EM structure of a single subunit of a Counterclockwise-locked form of the Salmonella enterica Typhimurium flagellar C-ring.

8UMD の概要

• エントリーDOI: 10.2210/pdb8umd/pdb
• EMDBエントリー: 42376
• 分子名称: Flagellar M-ring protein, Flagellar motor switch protein FliG, Flagellar motor switch protein FliM, ... (4 entities in total)
• 機能のキーワード: flagella, c-ring, salmonella, motor, rotation, motor protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 180493.14

構造登録者

Johnson, S.,Deme, J.C.,Lea, S.M. (登録日: 2023-10-17, 公開日: 2024-01-24, 最終更新日: 2024-05-22)

主引用文献

Johnson, S.,Deme, J.C.,Furlong, E.J.,Caesar, J.J.E.,Chevance, F.F.V.,Hughes, K.T.,Lea, S.M.
Structural basis of directional switching by the bacterial flagellum.
Nat Microbiol, 9:1282-1292, 2024

PubMed Abstract: The bacterial flagellum is a macromolecular protein complex that harvests energy from uni-directional ion flow across the inner membrane to power bacterial swimming via rotation of the flagellar filament. Rotation is bi-directional, with binding of a cytoplasmic chemotactic response regulator controlling reversal, though the structural and mechanistic bases for rotational switching are not well understood. Here we present cryoelectron microscopy structures of intact Salmonella flagellar basal bodies (3.2-5.5 Å), including the cytoplasmic C-ring complexes required for power transmission, in both counter-clockwise and clockwise rotational conformations. These reveal 180° movements of both the N- and C-terminal domains of the FliG protein, which, when combined with a high-resolution cryoelectron microscopy structure of the MotAB stator, show that the stator shifts from the outside to the inside of the C-ring. This enables rotational switching and reveals how uni-directional ion flow across the inner membrane is used to accomplish bi-directional rotation of the flagellum.

PubMed: 38459206
DOI: 10.1038/s41564-024-01630-z

実験手法

ELECTRON MICROSCOPY (3.6 Å)