ArticleNature communications2023
Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.Nature communications · 2026Article
- Heterogeneity and multi-scale dynamics in the molecular bearing of the bacterial flagellum.Nature communications · 2026Article
- Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026Review
- Article
- Insertion of Fluorescent Proteins Near the Plug Domain of MotB Generates Functional Stator Complexes.MicrobiologyOpen · 2025Article
- Cryo-EM structures of the E. coli Ton and Tol motor complexes.Nature communications · 2025Article
- Chemotaxis and Related Signaling Systems inBiomolecules · 2025Review
- Cryo-EM Structure of the Flagellar Motor Complex fromBiomolecules · 2025Article
- Modularity of Zorya defense systems during phage inhibition.Nature communications · 2025Article
- Article
- Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS fromBiomolecules · 2025Article
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
- Structural insight into sodium ion pathway in the bacterial flagellar stator from marineProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A very versatile molecular machine.Journal of bacteriology · 2024Article
- Hybrid Exb/Mot stators require substitutions distant from the chimeric pore to power flagellar rotation.Journal of bacteriology · 2024Article
- Theoretical insights into rotary mechanism of MotAB in the bacterial flagellar motor.Biophysical journal · 2024Article
- Structure, function, and biophysics of bacterial motility and the flagellar motor-IUPAB2024 session commentary.Biophysical reviews · 2024Article
- CryoEM structures reveal how the bacterial flagellum rotates and switches direction.Nature microbiology · 2024Article
- Membrane platform protein PulF of themBio · 2024Article
- Tuning the stator subunit of the flagellar motor with coiled-coil engineering.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
11 authors.
Funding
Abstract
Bacteria swim using a flagellar motor that is powered by stator units. Vibrio spp. are highly motile bacteria responsible for various human diseases, the polar flagella of which are exclusively driven by sodium-dependent stator units (PomAB). However, how ion selectivity is attained, how ion transport triggers the directional rotation of the stator unit, and how the stator unit is incorporated into the flagellar rotor remained largely unclear. Here, we have determined by cryo-electron microscopy the structure of Vibrio PomAB. The electrostatic potential map uncovers sodium binding sites, which together with functional experiments and molecular dynamics simulations, reveal a mechanism for ion translocation and selectivity. Bulky hydrophobic residues from PomA prime PomA for clockwise rotation. We propose that a dynamic helical motif in PomA regulates the distance between PomA subunit cytoplasmic domains, stator unit activation, and torque transmission. Together, our study provides mechanistic insights for understanding ion selectivity and rotor incorporation of the stator unit of the bacterial flagellum.
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