ArticlePloS one2013
Flexibility within the rotor and stators of the vacuolar H+-ATPase.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- ModeHunter: A Package for the Reductionist Analysis, Animation, and Application of Elastic Biomolecular Motion.The journal of physical chemistry. B · 2025Article
- Changes within the central stalk of E. coli FCommunications biology · 2023Article
- Hands on Methods for High Resolution Cryo-Electron Microscopy Structures of Heterogeneous Macromolecular Complexes.Frontiers in molecular biosciences · 2019Review
- Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.Proteins · 2016Article
- Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.Science advances · 2016Review
- Methods to account for movement and flexibility in cryo-EM data processing.Methods (San Diego, Calif.) · 2016Article
- The changing landscape of membrane protein structural biology through developments in electron microscopy.Molecular membrane biology · 2016Review
- Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights.Structure (London, England : 1993) · 2015Article
- A new V-ATPase regulatory mechanism mediated by the Rab interacting lysosomal protein (RILP).Communicative & integrative biology · 2014Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
The V-ATPase is a membrane-bound protein complex which pumps protons across the membrane to generate a large proton motive force through the coupling of an ATP-driven 3-stroke rotary motor (V1) to a multistroke proton pump (Vo). This is done with near 100% efficiency, which is achieved in part by flexibility within the central rotor axle and stator connections, allowing the system to flex to minimise the free energy loss of conformational changes during catalysis. We have used electron microscopy to reveal distinctive bending along the V-ATPase complex, leading to angular displacement of the V1 domain relative to the Vo domain to a maximum of ~30°. This has been complemented by elastic network normal mode analysis that shows both flexing and twisting with the compliance being located in the rotor axle, stator filaments, or both. This study provides direct evidence of flexibility within the V-ATPase and by implication in related rotary ATPases, a feature predicted to be important for regulation and their high energetic efficiencies.
Indexed as
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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.