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-Structure paper
タイトル | Structural basis of directional switching by the bacterial flagellum. |
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ジャーナル・号・ページ | Nat Microbiol, Vol. 9, Issue 5, Page 1282-1292, Year 2024 |
掲載日 | 2024年3月8日 |
著者 | Steven Johnson / Justin C Deme / Emily J Furlong / Joseph J E Caesar / Fabienne F V Chevance / Kelly T Hughes / Susan M Lea / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Microbiol / PubMed:38459206 |
手法 | EM (単粒子) |
解像度 | 2.4 - 5.4 Å |
構造データ | EMDB-42139, PDB-8ucs: EMDB-42376, PDB-8umd: EMDB-42387, PDB-8umx: EMDB-42439, PDB-8uox: EMDB-42451, PDB-8upl: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | MEMBRANE PROTEIN / flagella chemotaxis motility type III secretion system / MOTOR PROTEIN / Flagella / C-ring / Salmonella / motor / rotation |