ArticleEMBO reports2009
Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase.
Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 55 citations in OpenAlex.
- CryoEM Reveals the Complexity and Diversity of ATP Synthases.Frontiers in microbiology · 2022Review
- Genotypic and Phenotypic Characterization of Highly Alkaline-ResistantMicroorganisms · 2021Article
- Single-molecule analysis reveals rotational substeps and chemo-mechanical coupling scheme ofThe Journal of biological chemistry · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Metastable asymmetrical structure of a shaftless VScience advances · 2019Article
- A proteomic approach reveals the differential protein expression inJournal of ginseng research · 2018Article
- Structure and dynamics of rotary VCellular and molecular life sciences : CMLS · 2018Review
- Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.PLoS pathogens · 2017Article
- Rotation Mechanism of Molecular Motor VBiophysical journal · 2017Article
- In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Crystal structures of the ATP-binding and ADP-release dwells of the VNature communications · 2016Article
- Rotation of artificial rotor axles in rotary molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases.Science advances · 2016Review
- Operating principles of rotary molecular motors: differences between FBiophysics and physicobiology · 2016Review
- Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans.The Journal of biological chemistry · 2015Article
- Article
- Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights.Structure (London, England : 1993) · 2015Article
- Torque generation of Enterococcus hirae V-ATPase.The Journal of biological chemistry · 2014Article
- 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
- Basic properties of rotary dynamics of the molecular motor Enterococcus hirae V1-ATPase.The Journal of biological chemistry · 2013Article
Corrections and comments
- Commented on by
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report a crystallographic study of V1-ATPase, from Thermus thermophilus, which is a soluble component consisting of A, B, D and F subunits. The structure at 4.5 A resolution reveals inter-subunit interactions and nucleotide binding. In particular, the structure of the central stalk composed of D and F subunits was shown to be characteristic of V1-ATPases. Small conformational changes of respective subunits and significant rearrangement of the quaternary structure observed in the three AB pairs were related to the interaction with the straight central stalk. The rotation mechanism is discussed based on a structural comparison between V1-ATPases and F1-ATPases.
Indexed as
Identifiers
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.