- EMDB-43258: CW Flagellar Switch Complex with extra density - FliF, FliG, FliM... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-43258
タイトル
CW Flagellar Switch Complex with extra density - FliF, FliG, FliM, and FliN forming single subunit of the C-ring from Salmonella
マップデータ
試料
複合体: Flagellar C-ring single subunit containing FliF, FliG, FliM, and FliN
タンパク質・ペプチド: Flagellar M-ring protein
タンパク質・ペプチド: Flagellar motor switch protein FliG
タンパク質・ペプチド: Flagellar motor switch protein FliM
タンパク質・ペプチド: Flagellar motor switch protein FliN
キーワード
Domain Swap / Symmetry mismatch / Flagellar component / Switch complex / MOTOR PROTEIN
機能・相同性
機能・相同性情報
bacterial-type flagellum basal body, MS ring / bacterial-type flagellum basal body / bacterial-type flagellum-dependent swarming motility / positive chemotaxis / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / chemotaxis / plasma membrane 類似検索 - 分子機能
Flagellar motor switch protein FliN, N-terminal / : / Flagellar motor switch protein FliN N-terminal / Flagellar motor switch FliN / Flagellar motor switch FliN/Type III secretion HrcQb / Flagellar motor switch protein FliG / Flagellar motor switch protein FliM / Flagellar motor switch protein FliG, alpha-helical / Flagellar motor switch protein FliG, C-terminal / Flagellar motor switch protein FliG, N-terminal domain ...Flagellar motor switch protein FliN, N-terminal / : / Flagellar motor switch protein FliN N-terminal / Flagellar motor switch FliN / Flagellar motor switch FliN/Type III secretion HrcQb / Flagellar motor switch protein FliG / Flagellar motor switch protein FliM / Flagellar motor switch protein FliG, alpha-helical / Flagellar motor switch protein FliG, C-terminal / Flagellar motor switch protein FliG, N-terminal domain / Flagellar motor switch protein FliG, middle domain / FliG C-terminal domain / Flagellar motor switch protein FliM / FliG middle domain / FliG N-terminal domain / CheC-like superfamily / Flagellar motor switch protein FliN-like, C-terminal domain / SpoA-like superfamily / Type III flagellar switch regulator (C-ring) FliN C-term / Flagellar M-ring protein FliF / Flagellar M-ring C-terminal / Flagellar M-ring protein C-terminal / Lipoprotein YscJ/Flagellar M-ring protein / Secretory protein of YscJ/FliF family / Flagellar M-ring , N-terminal / AMP-binding enzyme, C-terminal domain superfamily 類似検索 - ドメイン・相同性
Flagellar motor switch protein FliM / Flagellar motor switch protein FliG / Flagellar M-ring protein / Flagellar motor switch protein FliN 類似検索 - 構成要素
National Institutes of Health/John E. Fogarty International Center (NIH/FIC)
GM61606
米国
引用
ジャーナル: Nat Microbiol / 年: 2024 タイトル: CryoEM structures reveal how the bacterial flagellum rotates and switches direction. 著者: Prashant K Singh / Pankaj Sharma / Oshri Afanzar / Margo H Goldfarb / Elena Maklashina / Michael Eisenbach / Gary Cecchini / T M Iverson / 要旨: Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural ...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.