ArticleProceedings of the National Academy of Sciences of the United States of America2008
Insights into the stator assembly of the Vibrio flagellar motor from the crystal structure of MotY.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 71 citations in OpenAlex.
- Review
- Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.Nature communications · 2026Article
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- MotY modulates proton-driven flagellar motor output in Pseudomonas aeruginosa.BMC microbiology · 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
- Putative Spanner Function of theJournal of bacteriology · 2021Article
- Structure of the molecular bushing of the bacterial flagellar motor.Nature communications · 2021Article
- The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors.Frontiers in microbiology · 2021Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Article
- Molecular architecture of the sheathed polar flagellum inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural differences in the bacterial flagellar motor among bacterial species.Biophysics and physicobiology · 2017Review
- The tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacterium.Scientific reports · 2016Article
- Functional chimeras of flagellar stator proteins between E. coli MotB and Vibrio PomB at the periplasmic region in Vibrio or E. coli.MicrobiologyOpen · 2015Article
- 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
- Structure, gene regulation and environmental response of flagella in Vibrio.Frontiers in microbiology · 2013Article
- A quinazoline-2,4-diamino analog suppresses Vibrio cholerae flagellar motility by interacting with motor protein PomB and induces envelope stress.Antimicrobial agents and chemotherapy · 2013Article
- Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotation of the sodium-driven polar flagellum of Vibrio alginolyticus requires four motor proteins: PomA, PomB, MotX, and MotY. PomA and PomB form a sodium-ion channel in the cytoplasmic membrane that functions as a stator complex to couple sodium-ion flux with torque generation. MotX and MotY are components of the T-ring, which is located beneath the P-ring of the polar flagellar basal body and is involved in incorporation of the PomA/PomB complex into the motor. Here, we describe the determination of the crystal structure of MotY at 2.9 A resolution. The structure shows two distinct domains: an N-terminal domain (MotY-N) and a C-terminal domain (MotY-C). MotY-N has a unique structure. MotY-C contains a putative peptidoglycan-binding motif that is remarkably similar to those of peptidoglycan-binding proteins, such as Pal and RmpM, but this region is disordered in MotY. Motility assay of cells producing either of the MotY-N and MotY-C fragments and subsequent biochemical analyses indicate that MotY-N is essential for association of the stator units around the rotor, whereas MotY-C stabilizes the association by binding to the peptidoglycan layer. Based on these observations, we propose a model for the mechanism of stator assembly around the rotor.
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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.