ArticleCell research2024
Structural basis of the bacterial flagellar motor rotational switching.
Article in Cell research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Molecular basis of high-torque transmission of the Vibrio polar flagellar motor.Protein & cell · 2026Article
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- A quantum-mechanical framework for million-atom scale biological systems.Communications chemistry · 2026Article
- Article
- Understanding c-di-GMP-mediated regulation of flagellar motility, one step at a time.Journal of bacteriology · 2026Article
- Ultrastructure Analysis by Cryo-Electron Tomography Revealed Mesosomes in the Gram-negative Delftia Acidovorans.Microbial ecology · 2026Article
- Article
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Texas 2-step: a new model for YcgR::c-di-GMP action at the flagellar motor.Journal of bacteriology · 2025Article
- Torque-generating units of the bacterial flagellar motor are rotary motors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Texas 2-Step: A new Model for YcgR::c-di-GMP Action at the Flagellar Motor.bioRxiv : the preprint server for biology · 2025Article
- Article
- Bridging Quantum Mechanics and Biology at the Million-Atom Scale.Research square · 2025Article
- Genome-wide analysis of Burkholderia for the management of antimicrobial-resistant in cystic fibrosis patients.AMB Express · 2025Article
- A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque.Nature microbiology · 2025Article
- Improving CryoEM maps of symmetry-mismatched macromolecular assemblies: A case study on the flagellar motor.Journal of structural biology · 2025Article
- Proteomic Analysis Reveals the Phenotypic Heterogeneity and Tolerance Mechanisms of HalophilicBiomolecules · 2025Article
- Scrutinizing Stator Rotation in the Bacterial Flagellum: Reconciling Experiments and Switching Models.Biomolecules · 2025Review
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
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6 authors.
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Abstract
The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive. Here, we present two high-resolution cryo-electron microscopy structures of the C ring-containing flagellar basal body-hook complex from Salmonella Typhimurium, which are in the default counterclockwise state and in a constitutively active CheY mutant-induced clockwise state, respectively. In both complexes, the C ring consists of four subrings, but is in two different conformations. The CheY proteins are bound into an open groove between two adjacent protomers on the surface of the middle subring of the C ring and interact with the FliG and FliM subunits. The binding of the CheY protein induces a significant upward shift of the C ring towards the MS ring and inward movements of its protomers towards the motor center, which eventually remodels the structures of the FliG subunits and reverses the orientations and surface electrostatic potential of the α
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