Journal
NATURE MICROBIOLOGY
Volume 5, Issue 12, Pages 1553-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41564-020-0788-8
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Funding
- Wellcome Trust [208361/Z/17/Z, 201536, 100298, 209194, 107929/Z/15/Z]
- EPA Cephalosporin Trust
- Wolfson Foundation
- Royal Society/Wolfson Foundation Laboratory Refurbishment Grant [WL160052]
- Medical Research Council (MRC) Programme Grant [MR/M011984/1]
- Canadian Institutes of Health Research [178048-BMA-CFAA-11449]
- MRC [MR/S009213/1]
- BBSRC [BB/P01948X/1, BB/R002517/1, BB/S003339/1]
- Engineering and Physical Sciences Research Council (EPSRC) [EP/R029407/1]
- EPSRC [EP/P020232/1]
- MRC [MR/S021264/1, MR/M011984/1] Funding Source: UKRI
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Using single-particle analysis cryogenic electron microscopy, the authors determine the structures of the bacterial flagellum stator complexes from three diverse bacteria. The bacterial flagellum is the prototypical protein nanomachine and comprises a rotating helical propeller attached to a membrane-embedded motor complex. The motor consists of a central rotor surrounded by stator units that couple ion flow across the cytoplasmic membrane to generate torque. Here, we present the structures of the stator complexes fromClostridium sporogenes,Bacillus subtilisandVibrio mimicus, allowing interpretation of the extensive body of data on stator mechanism. The structures reveal an unexpected asymmetric A(5)B(2)subunit assembly where the five A subunits enclose the two B subunits. Comparison to structures of other ion-driven motors indicates that this A(5)B(2)architecture is fundamental to bacterial systems that couple energy from ion flow to generate mechanical work at a distance and suggests that such events involve rotation in the motor structures.
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