ArticleProceedings of the National Academy of Sciences of the United States of America2015
Gate-controlled proton diffusion and protonation-induced ratchet motion in the stator of the bacterial flagellar motor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Scrutinizing Stator Rotation in the Bacterial Flagellum: Reconciling Experiments and Switching Models.Biomolecules · 2025Review
- Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors.Journal of molecular evolution · 2023Article
- Ion-Powered Rotary Motors: Where Did They Come from and Where They Are Going?International journal of molecular sciences · 2023Review
- Role of salt-bridging interactions in recognition of viral RNA by arginine-rich peptides.Biophysical journal · 2021Article
- Structural basis of bacterial flagellar motor rotation and switching.Trends in microbiology · 2021Review
- The Dynamic Ion Motive Force Powering the Bacterial Flagellar Motor.Frontiers in microbiology · 2021Review
- Expansion of Necrosis Depending on Hybrid Motor-Driven Motility ofMicroorganisms · 2020Article
- Structures of the stator complex that drives rotation of the bacterial flagellum.Nature microbiology · 2020Article
- Evolution of the Stator Elements of Rotary Prokaryote Motors.Journal of bacteriology · 2020Review
- Dynamic exchange of two types of stator units inComputational and structural biotechnology journal · 2020Review
- Voltage vs. Ligand II: Structural insights of the intrinsic flexibility in cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2019Article
- Functional Regulators of Bacterial Flagella.Annual review of microbiology · 2019Review
- Essential ion binding residues for NaScientific reports · 2019Article
- Flagella-Driven Motility of Bacteria.Biomolecules · 2019Review
- Effect of the MotA(M206I) Mutation on Torque Generation and Stator Assembly in theJournal of bacteriology · 2019Article
- Molecular dynamics simulation of bacterial flagella.Biophysical reviews · 2018Review
- SwrD (YlzI) Promotes Swarming in Bacillus subtilis by Increasing Power to Flagellar Motors.Journal of bacteriology · 2018Article
- NaScience advances · 2017Article
- Some Liked It Hot: A Hypothesis Regarding Establishment of the Proto-Mitochondrial Endosymbiont During Eukaryogenesis.Journal of molecular evolution · 2017Review
- Bacteria, Rev Your Engines: Stator Dynamics Regulate Flagellar Motility.Journal of bacteriology · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proton permeation process of the stator complex MotA/B in the flagellar motor of Escherichia coli was investigated. The atomic model structure of the transmembrane part of MotA/B was constructed based on the previously published disulfide cross-linking and tryptophan scanning mutations. The dynamic permeation of hydronium/sodium ions and water molecule through the channel formed in MotA/B was observed using a steered molecular dynamics simulation. During the simulation, Leu46 of MotB acts as the gate for hydronium ion permeation, which induced the formation of water wire that may mediate the proton transfer to Asp32 on MotB. Free energy profiles for permeation were calculated by umbrella sampling. The free energy barrier for H3O(+) permeation was consistent with the proton transfer rate deduced from the flagellar rotational speed and number of protons per rotation, which suggests that the gating is the rate-limiting step. Structure and dynamics of the MotA/B with nonprotonated and protonated Asp32, Val43Met, and Val43Leu mutants in MotB were investigated using molecular dynamics simulation. A narrowing of the channel was observed in the mutants, which is consistent with the size-dependent ion selectivity. In MotA/B with the nonprotonated Asp32, the A3 segment in MotA maintained a kink whereas the protonation induced a straighter shape. Assuming that the cytoplasmic domain not included in the atomic model moves as a rigid body, the protonation/deprotonation of Asp32 is inferred to induce a ratchet motion of the cytoplasmic domain, which may be correlated to the motion of the flagellar rotor.
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