ArticleProceedings of the National Academy of Sciences of the United States of America2014
Conformational change in the periplamic region of the flagellar stator coupled with the assembly around the rotor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
46 citing papers in PubMed, 95 citations in OpenAlex.
- Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.Nature communications · 2026Article
- Long-range coupling regulates stator dynamics in the bacterial flagellar motor.bioRxiv : the preprint server for biology · 2025Article
- Signature of cooperativity in the stochastic fluctuations of small systems with application to the bacterial flagellar motor.Scientific reports · 2025Article
- Article
- Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS fromBiomolecules · 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
- Viscosity-dependent determinants ofmBio · 2024Article
- Article
- FliL and its paralog MotF have distinct roles in the stator activity of the Sinorhizobium meliloti flagellar motor.Molecular microbiology · 2022Article
- Relaxation time asymmetry in stator dynamics of the bacterial flagellar motor.Science advances · 2022Article
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- Bacterial Proprioception: Can a Bacterium Sense Its Movement?Frontiers in microbiology · 2022Review
- The Bacterial Flagellar Motor: Insights Into Torque Generation, Rotational Switching, and Mechanosensing.Frontiers in microbiology · 2022Review
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- Dynamic Hybrid Flagellar Motors-Fuel Switch and More.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
- Structures of the stator complex that drives rotation of the bacterial flagellum.Nature microbiology · 2020Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The torque of the bacterial flagellum is generated by the rotor-stator interaction coupled with the ion flow through the channel in the stator. Anchoring the stator unit to the peptidoglycan layer with proper orientation around the rotor is believed to be essential for smooth rotation of the flagellar motor. The stator unit of the sodium-driven flagellar motor of Vibrio is composed of PomA and PomB, and is thought to be fixed to the peptidoglycan layer and the T-ring by the C-terminal periplasmic region of PomB. Here, we report the crystal structure of a C-terminal fragment of PomB (PomBC) at 2.0-Å resolution, and the structure suggests a conformational change in the N-terminal region of PomBC for anchoring the stator. On the basis of the structure, we designed double-Cys replaced mutants of PomB for in vivo disulfide cross-linking experiments and examined their motility. The motility can be controlled reproducibly by reducing reagent. The results of these experiments suggest that the N-terminal disordered region (121-153) and following the N-terminal two-thirds of α1(154-164) in PomBC changes its conformation to form a functional stator around the rotor. The cross-linking did not affect the localization of the stator nor the ion conductivity, suggesting that the conformational change occurs in the final step of the stator assembly around the rotor.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.