8UMD
Cryo-EM structure of a single subunit of a Counterclockwise-locked form of the Salmonella enterica Typhimurium flagellar C-ring.
Summary for 8UMD
| Entry DOI | 10.2210/pdb8umd/pdb |
| EMDB information | 42376 |
| Descriptor | Flagellar M-ring protein, Flagellar motor switch protein FliG, Flagellar motor switch protein FliM, ... (4 entities in total) |
| Functional Keywords | flagella, c-ring, salmonella, motor, rotation, motor protein |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium More |
| Total number of polymer chains | 6 |
| Total formula weight | 180493.14 |
| Authors | Johnson, S.,Deme, J.C.,Lea, S.M. (deposition date: 2023-10-17, release date: 2024-01-24, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 38459206DOI: 10.1038/s41564-024-01630-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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