ArticleNature microbiology2024
CryoEM structures reveal how the bacterial flagellum rotates and switches direction.
Article in Nature microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Heterogeneity and multi-scale dynamics in the molecular bearing of the bacterial flagellum.Nature communications · 2026Article
- Osmotic stress triggers fast and reversible PMF collapse in Escherichia coli.Biophysical journal · 2026Article
- Understanding c-di-GMP-mediated regulation of flagellar motility, one step at a time.Journal of bacteriology · 2026Article
- The dynamic response of the bacterial flagellar motor to its direct intracellular input signal.Proceedings of the National Academy of Sciences of the United States of America · 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
- 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
- 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
- Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries.Communications biology · 2025Article
- Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A year of microbiology.Nature microbiology · 2024Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- Structural basis of the bacterial flagellar motor rotational switching.Cell research · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 Å) and isolated C-ring in a clockwise pose alone (4.6 Å) and bound to a regulator (5.9 Å). Conformational differences between rotational poses include a 180° shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation.
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