8VKR

CW Flagellar Switch Complex with extra density - FliF, FliG, FliM, and FliN forming the C-ring from Salmonella

これはPDB形式変換不可エントリーです。

8VKR の概要

• エントリーDOI: 10.2210/pdb8vkr/pdb
• EMDBエントリー: 43328
• 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: domain swap, symmetry mismatch, flagellar component, switch complex, 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: 204
• 化学式量合計: 5968867.93

構造登録者

Singh, P.K.,Iverson, T.M. (登録日: 2024-01-09, 公開日: 2024-02-28, 最終更新日: 2024-08-21)

主引用文献

Singh, P.K.,Sharma, P.,Afanzar, O.,Goldfarb, M.H.,Maklashina, E.,Eisenbach, M.,Cecchini, G.,Iverson, T.M.
CryoEM structures reveal how the bacterial flagellum rotates and switches direction.
Nat Microbiol, 9:1271-1281, 2024

PubMed Abstract: Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 Å) and isolated C-ring in a clockwise pose alone (4.6 Å) and bound to a regulator (5.9 Å). Conformational differences between rotational poses include a 180° shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation.

PubMed: 38632342
DOI: 10.1038/s41564-024-01674-1

実験手法

ELECTRON MICROSCOPY (5.9 Å)