ArticleProceedings of the National Academy of Sciences of the United States of America2013
Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 55 citations in OpenAlex.
- Molecular basis of high-torque transmission of the Vibrio polar flagellar motor.Protein & cell · 2026Article
- Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.Nature communications · 2026Article
- In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque.Nature microbiology · 2025Article
- Chemotaxis and Related Signaling Systems inBiomolecules · 2025Review
- A Helicobacter pylori flagellar motor accessory is needed to maintain the barrier function of the outer membrane during flagellar rotation.PLoS pathogens · 2025Article
- Molecular model of a bacterial flagellar motorbioRxiv : the preprint server for biology · 2024Article
- Viscosity-dependent determinants ofmBio · 2024Article
- The Vibrio Polar Flagellum: Structure and Regulation.Advances in experimental medicine and biology · 2023Article
- Structure and Assembly of the Bacterial Flagellum.Sub-cellular biochemistry · 2022Review
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors.Frontiers in microbiology · 2021Review
- The Dynamic Ion Motive Force Powering the Bacterial Flagellar Motor.Frontiers in microbiology · 2021Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Article
- Evolution of the Stator Elements of Rotary Prokaryote Motors.Journal of bacteriology · 2020Review
- Article
- γ-proteobacteria eject their polar flagella under nutrient depletion, retaining flagellar motor relic structures.PLoS biology · 2019Article
- The presence and absence of periplasmic rings in bacterial flagellar motors correlates with stator type.eLife · 2019Article
- The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum.Journal of bacteriology · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flagellar motility is a key factor for bacterial survival and growth in fluctuating environments. The polar flagellum of a marine bacterium, Vibrio alginolyticus, is driven by sodium ion influx and rotates approximately six times faster than the proton-driven motor of Escherichia coli. The basal body of the sodium motor has two unique ring structures, the T ring and the H ring. These structures are essential for proper assembly of the stator unit into the basal body and to stabilize the motor. FlgT, which is a flagellar protein specific for Vibrio sp., is required to form and stabilize both ring structures. Here, we report the crystal structure of FlgT at 2.0-Å resolution. FlgT is composed of three domains, the N-terminal domain (FlgT-N), the middle domain (FlgT-M), and the C-terminal domain (FlgT-C). FlgT-M is similar to the N-terminal domain of TolB, and FlgT-C resembles the N-terminal domain of FliI and the α/β subunits of F1-ATPase. To elucidate the role of each domain, we prepared domain deletion mutants of FlgT and analyzed their effects on the basal-body ring formation. The results suggest that FlgT-N contributes to the construction of the H-ring structure, and FlgT-M mediates the T-ring association on the LP ring. FlgT-C is not essential but stabilizes the H-ring structure. On the basis of these results, we propose an assembly mechanism for the basal-body rings and the stator units of the sodium-driven flagellar motor.
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