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TitleStructural basis of directional switching by the bacterial flagellum.
Journal, issue, pagesNat Microbiol, Vol. 9, Issue 5, Page 1282-1292, Year 2024
Publish dateMar 8, 2024
AuthorsSteven Johnson / Justin C Deme / Emily J Furlong / Joseph J E Caesar / Fabienne F V Chevance / Kelly T Hughes / Susan M Lea /
PubMed AbstractThe 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.
External linksNat Microbiol / PubMed:38459206
MethodsEM (single particle)
Resolution2.4 - 5.4 Å
Structure data

42139

8ucs

EMDB-42139, PDB-8ucs:
Cryo-EM structure of the flagellar MotAB stator bound to FliG
Method: EM (single particle) / Resolution: 2.4 Å

42376

8umd

EMDB-42376, PDB-8umd:
Cryo-EM structure of a single subunit of a Counterclockwise-locked form of the Salmonella enterica Typhimurium flagellar C-ring.
Method: EM (single particle) / Resolution: 3.6 Å

42387

8umx

EMDB-42387, PDB-8umx:
Cryo-EM structure of a single subunit of a Clockwise-locked form of the Salmonella enterica Typhimurium flagellar C-ring.
Method: EM (single particle) / Resolution: 4.0 Å

42439

8uox

EMDB-42439, PDB-8uox:
Cryo-EM structure of a Counterclockwise locked form of the Salmonella enterica Typhimurium flagellar C-ring, with C34 symmetry applied
Method: EM (single particle) / Resolution: 4.6 Å

42451

8upl

EMDB-42451, PDB-8upl:
Cryo-EM structure of a Clockwise locked form of the Salmonella enterica Typhimurium flagellar C-ring, with C34 symmetry applied
Method: EM (single particle) / Resolution: 5.4 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • clostridium sporogenes (bacteria)
  • salmonella enterica subsp. enterica serovar typhimurium (bacteria)
KeywordsMEMBRANE PROTEIN / flagella chemotaxis motility type III secretion system / MOTOR PROTEIN / Flagella / C-ring / Salmonella / motor / rotation

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