8ucs | pdb_00008ucs

Cryo-EM structure of the flagellar MotAB stator bound to FliG

spinqualitylabelsall models 8ucs, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ucs is a 10 chain structure with sequence from Clostridium sporogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1V9IL35_CLOSG Publication Abstract from PubMed 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 A), including the cytoplasmic C-ring complexes required for power transmission, in both counter-clockwise and clockwise rotational conformations. These reveal 180 degrees 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 MotA(5)B(2) 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. Structural basis of directional switching by the bacterial flagellum.,Johnson S, Deme JC, Furlong EJ, Caesar JJE, Chevance FFV, Hughes KT, Lea SM Nat Microbiol. 2024 May;9(5):1282-1292. doi: 10.1038/s41564-024-01630-z. Epub , 2024 Mar 8. PMID:38459206 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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