ArticleProceedings of the National Academy of Sciences of the United States of America2016
Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 50 citations in OpenAlex.
- Influence of creatine pyruvate on newly received cattle: insights from metagenomics and metabolomics.BMC microbiology · 2025Article
- Dietary selection of distinct gastrointestinal microorganisms drives fiber utilization dynamics in goats.Microbiome · 2025Article
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Determination of the Cryo-EM Structure of ATG9 from Arabidopsis thaliana.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover.Communications biology · 2023Article
- Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023Review
- Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?Frontiers in molecular biosciences · 2023Review
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Application of Homology Modeling by Enhanced Profile-Profile Alignment and Flexible-Fitting Simulation to Cryo-EM Based Structure Determination.International journal of molecular sciences · 2022Article
- CryoEM Reveals the Complexity and Diversity of ATP Synthases.Frontiers in microbiology · 2022Review
- Article
- Cryo-EM structures of intact V-ATPase from bovine brain.Nature communications · 2020Article
- Mechanical inhibition of isolated VeLife · 2020Article
- Subnanometer resolution cryo-EM structure ofAutophagy · 2020Article
- Single-molecule analysis reveals rotational substeps and chemo-mechanical coupling scheme ofThe Journal of biological chemistry · 2019Article
- Structure Determination by Single-Particle Cryo-Electron Microscopy: Only the Sky (and Intrinsic Disorder) is the Limit.International journal of molecular sciences · 2019Review
- Structural comparison of the vacuolar and Golgi V-ATPases fromProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Vacuolar-type ATPase: A proton pump to lysosomal trafficking.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy.Scientific reports · 2018Article
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3 authors at 1 institution in 1 country.
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Abstract
Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the membrane-embedded a subunit. The V/A-ATPase from the eubacterium Thermus thermophilus is similar in structure to the eukaryotic V-ATPase but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. We determined the T. thermophilus V/A-ATPase structure by cryo-EM at 6.4 Å resolution. Evolutionary covariance analysis allowed tracing of the a subunit sequence within the map, providing a complete model of the rotary ATPase. Comparing the membrane-embedded regions of the T. thermophilus V/A-ATPase and eukaryotic V-ATPase from Saccharomyces cerevisiae allowed identification of the α-helices that belong to the a subunit and revealed the existence of previously unknown subunits in the eukaryotic enzyme. Subsequent evolutionary covariance analysis enabled construction of a model of the a subunit in the S. cerevisae V-ATPase that explains numerous biochemical studies of that enzyme. Comparing the two a subunit structures determined here with a structure of the distantly related a subunit from the bovine F-type ATP synthase revealed a conserved pattern of residues, suggesting a common mechanism for proton transport in all rotary ATPases.
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