ArticleStructure (London, England : 1993)2015
Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Reversible binding of divalent cations toFrontiers in molecular biosciences · 2023Review
- Schisandrol A protects AGEs-induced neuronal cells death by allosterically targeting ATP6V0d1 subunit of V-ATPase.Acta pharmaceutica Sinica. B · 2022Article
- Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.Molecular cell · 2020Article
- A cation-π interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment.The Journal of biological chemistry · 2018Article
- MgATP hydrolysis destabilizes the interaction between subunit H and yeast VThe Journal of biological chemistry · 2018Article
- Approaches to altering particle distributions in cryo-electron microscopy sample preparation.Acta crystallographica. Section D, Structural biology · 2018Review
- Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.PLoS pathogens · 2017Article
- Breaking up and making up: The secret life of the vacuolar HProtein science : a publication of the Protein Society · 2017Review
- Comparative molecular analyses of select pH- and osmoregulatory genes in three freshwater crayfishPeerJ · 2017Article
- Disorders of lysosomal acidification-The emerging role of v-ATPase in aging and neurodegenerative disease.Ageing research reviews · 2016Review
- Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.Proteins · 2016Article
- Relating proton pumps with gap junctions: colocalization of ductin, the channel-forming subunit c of V-ATPase, with subunit a and with innexins 2 and 3 during Drosophila oogenesis.BMC developmental biology · 2016Article
- Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.Science advances · 2016Review
- Rotating with the brakes on and other unresolved features of the vacuolar ATPase.Biochemical Society transactions · 2016Review
- An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology.Methods (San Diego, Calif.) · 2016Article
- Methods to account for movement and flexibility in cryo-EM data processing.Methods (San Diego, Calif.) · 2016Article
- Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore.Scientific reports · 2016Article
- The changing landscape of membrane protein structural biology through developments in electron microscopy.Molecular membrane biology · 2016Review
- Control of lysosomal biogenesis and Notch-dependent tissue patterning by components of the TFEB-V-ATPase axis in Drosophila melanogaster.Autophagy · 2016Article
- Molecular Interactions and Cellular Itinerary of the Yeast RAVE (Regulator of the H+-ATPase of Vacuolar and Endosomal Membranes) Complex.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors.
Funding
Abstract
Vacuolar H(+)-ATPases are multisubunit complexes that operate with rotary mechanics and are essential for membrane proton transport throughout eukaryotes. Here we report a ∼ 1 nm resolution reconstruction of a V-ATPase in a different conformational state from that previously reported for a lower-resolution yeast model. The stator network of the V-ATPase (and by implication that of other rotary ATPases) does not change conformation in different catalytic states, and hence must be relatively rigid. We also demonstrate that a conserved bearing in the catalytic domain is electrostatic, contributing to the extraordinarily high efficiency of rotary ATPases. Analysis of the rotor axle/membrane pump interface suggests how rotary ATPases accommodate different c ring stoichiometries while maintaining high efficiency. The model provides evidence for a half channel in the proton pump, supporting theoretical models of ion translocation. Our refined model therefore provides new insights into the structure and mechanics of the V-ATPases.
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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.