ArticleThe EMBO journal2005
Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Population structure and gene flux ofMicrobial genomics · 2025Article
- Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.The Journal of biological chemistry · 2023Article
- Structures of multisubunit membrane complexes with the CRYO ARM 200.Microscopy (Oxford, England) · 2022Article
- Mechanical inhibition of isolated VeLife · 2020Article
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- Single-Nanoparticle Tracking with Angstrom Localization Precision and Microsecond Time Resolution.Biophysical journal · 2018Article
- Cryo EM structure of intact rotary HNature communications · 2018Article
- Rotation of artificial rotor axles in rotary molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Rotating with the brakes on and other unresolved features of the vacuolar ATPase.Biochemical Society transactions · 2016Review
- Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights.Structure (London, England : 1993) · 2015Article
- 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
- Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus.PloS one · 2013Article
- Single-molecule analysis of inhibitory pausing states of V1-ATPase.The Journal of biological chemistry · 2012Article
- Reconstitution of vacuolar-type rotary H+-ATPase/synthase from Thermus thermophilus.The Journal of biological chemistry · 2012Article
- Cloning and overexpression of an important functional gene ATP6V1F encoding a component of vacuolar ATPase from the Giant Panda (Ailuropoda melanoleuca).Molecular biology reports · 2012Article
- Crystal structure of the central axis DF complex of the prokaryotic V-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- Regulation and isoform function of the V-ATPases.Biochemistry · 2010Review
- The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase.Nature structural & molecular biology · 2010Article
- Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase.EMBO reports · 2009Article
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Authors and funding
12 authors.
Funding
Abstract
The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY. The structure was successfully placed into the low-resolution EM structure of the prokaryotic holo-V-ATPase at a location indicated by the results of crosslinking experiments. The crystal structure, together with the single-molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a 'retracted' form in the absence and an 'extended' form in the presence of ATP. Our results postulated that the subunit F is a regulatory subunit in the V-ATPase.
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