ArticleJournal of bacteriology2011
Structure of the flagellar motor protein complex PomAB: implications for the torque-generating conformation.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- Article
- MotY modulates proton-driven flagellar motor output in Pseudomonas aeruginosa.BMC microbiology · 2024Article
- Ion-Powered Rotary Motors: Where Did They Come from and Where They Are Going?International journal of molecular sciences · 2023Review
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Bacterial Flagellar Motor: Insights Into Torque Generation, Rotational Switching, and Mechanosensing.Frontiers in microbiology · 2022Review
- Putative Spanner Function of theJournal of bacteriology · 2021Article
- Site-directed crosslinking identifies the stator-rotor interaction surfaces in a hybrid bacterial flagellar motor.Journal of bacteriology · 2021Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Article
- Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020Review
- Article
- Evolution of higher torque in Campylobacter-type bacterial flagellar motors.Scientific reports · 2018Article
- Catch bond drives stator mechanosensitivity in the bacterial flagellar motor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.Scientific reports · 2017Article
- Imaging the motility and chemotaxis machineries in Helicobacter pylori by cryo-electron tomography.Journal of bacteriology · 2017Article
- The tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacterium.Scientific reports · 2016Article
- Diverse high-torque bacterial flagellar motors assemble wider stator rings using a conserved protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Conformational change in the periplamic region of the flagellar stator coupled with the assembly around the rotor.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Contribution of many charged residues at the stator-rotor interface of the Na+-driven flagellar motor to torque generation in Vibrio alginolyticus.Journal of bacteriology · 2014Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial flagellar motor is driven by an ion flux through a channel called MotAB in Escherichia coli or Salmonella and PomAB in Vibrio alginolyticus. PomAB is composed of two transmembrane (TM) components, PomA and PomB, and converts a sodium ion flux to rotation of the flagellum. Its homolog, MotAB, utilizes protons instead of sodium ions. PomB/MotB has a peptidoglycan (PG)-binding motif in the periplasmic domain, allowing it to function as the stator by being anchored to the PG layer. To generate torque, PomAB/MotAB is thought to undergo a conformational change triggered by the ion flux and to interact directly with FliG, a component of the rotor. Here, we present the first three-dimensional structure of this torque-generating stator unit analyzed by electron microscopy. The structure of PomAB revealed two arm domains, which contain the PG-binding site, connected to a large base made of the TM and cytoplasmic domains. The arms lean downward to the membrane surface, likely representing a "plugged" conformation, which would prevent ions leaking through the channel. We propose a model for how PomAB units are placed around the flagellar basal body to function as torque generators.
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