ArticleProceedings of the National Academy of Sciences of the United States of America2011
Crystal structure of the central axis DF complex of the prokaryotic V-ATPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- NaNature structural & molecular biology · 2025Article
- Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover.Communications biology · 2023Article
- Revealing a Hidden Intermediate of Rotatory Catalysis with X-ray Crystallography and Molecular Simulations.ACS central science · 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
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Rotational Mechanism Model of the Bacterial VFrontiers in physiology · 2019Review
- Metastable asymmetrical structure of a shaftless VScience advances · 2019Article
- Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy.Scientific reports · 2018Article
- Rotation Mechanism of Molecular Motor VBiophysical journal · 2017Article
- Crystal structures of the ATP-binding and ADP-release dwells of the VNature communications · 2016Article
- Operating principles of rotary molecular motors: differences between FBiophysics and physicobiology · 2016Review
- Recent Insights into the Structure, Regulation, and Function of the V-ATPases.Trends in biochemical sciences · 2015Review
- Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae.The Journal of biological chemistry · 2015Article
- The ingenious structure of central rotor apparatus in VoV1; key for both complex disassembly and energy coupling between V1 and Vo.PloS one · 2015Article
- Subunit positioning and stator filament stiffness in regulation and power transmission in the V1 motor of the Manduca sexta V-ATPase.Journal of molecular biology · 2014Article
- Molecular basis of ADP inhibition of vacuolar (V)-type ATPase/synthase.The Journal of biological chemistry · 2014Article
- Article
- Crystal and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae.The Journal of biological chemistry · 2013Article
- Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures.Nature · 2013Article
- Mechanical modulation of ATP-binding affinity of V1-ATPase.The Journal of biological chemistry · 2013Article
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Authors and funding
13 authors at 7 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V(1)-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A(3)B(3) complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.
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