ArticleNature microbiology2024
Structural basis of directional switching by the bacterial flagellum.
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 36 papers.
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Who cites it
36 citing papers in PubMed, 54 citations in OpenAlex.
- GeoPep: A Geometry-Aware Masked Language Model for Protein-Peptide Binding Site Prediction.Journal of chemical information and modeling · 2026Article
- 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
- Structural basis of outer membrane biogenesis and cell division by Tol/Pal nanomachinery.Science advances · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Article
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Role of FlhF and its domains in the assembly of a polar flagellum inJournal of bacteriology · 2025Article
- 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
- A shared mechanism for Bacteroidota protein transport and gliding motility.Nature communications · 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
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque.Nature microbiology · 2025Article
- The structure of the complete extracellular bacterial flagellum reveals the mechanism of flagellin incorporation.Nature microbiology · 2025Article
- Improving CryoEM maps of symmetry-mismatched macromolecular assemblies: A case study on the flagellar motor.Journal of structural biology · 2025Article
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
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 MotA
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.