Evidence map›Paper›PMID 25381992›Full record

ArticleNature communications2014

High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase.

Doreen Matthies, Wenchang Zhou, Adriana L Klyszejko, Claudio Anselmi, Özkan Yildiz, Karsten Brandt, Volker Müller, José D Faraldo-Gómez, Thomas Meier

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Secondary metabolites fromRSC advances · 2026
    Article
  3. Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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 · 2022
    Article
  9. Biosynthesis of butyrate from methanol and carbon monoxide by recombinant Acetobacterium woodii.International microbiology : the official journal of the Spanish Society for Microbiology · 2022
    Article
  10. ATP synthesis in an ancient ATP synthase at low driving forces.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. ATP synthase FCellular and molecular life sciences : CMLS · 2022
    Review
  12. Systems Biology on Acetogenic Bacteria for Utilizing C1 Feedstocks.Advances in biochemical engineering/biotechnology · 2022
    Article
  13. Review
  14. Article
  15. Overcoming Energetic Barriers in Acetogenic C1 Conversion.Frontiers in bioengineering and biotechnology · 2020
    Review
  16. Essential ion binding residues for NaScientific reports · 2019
    Article
  17. Review
  18. Genome-scale analysis ofRNA (New York, N.Y.) · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Doreen MatthiesDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Wenchang ZhouTheoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Building 5635FL, Suite T-800, Bethesda, Maryland 20892, USA.
Adriana L KlyszejkoDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Claudio AnselmiTheoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Building 5635FL, Suite T-800, Bethesda, Maryland 20892, USA.
Özkan YildizDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
Karsten BrandtDepartment of Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt am Main, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany.
Volker MüllerDepartment of Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt am Main, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany.
José D Faraldo-Gómez1] Theoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Building 5635FL, Suite T-800, Bethesda, Maryland 20892, USA [2] Cluster of Excellence Macromolecular Complexes, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany.
Thomas Meier1] Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany [2] Cluster of Excellence Macromolecular Complexes, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany.
Max Planck Institute of Biophysics · DEGoethe University Frankfurt · DENational Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Intramural NIH HHS Z99 HL999999
6 · The paper itself

Abstract

All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is coupled to the transmembrane flow of H(+) or Na(+). Physiologically, however, F/A-type enzymes specialize in ATP synthesis driven by downhill ion diffusion, while eukaryotic V-type ATPases function as ion pumps. To begin to rationalize the molecular basis for this functional differentiation, we solved the crystal structure of the Na(+)-driven membrane rotor of the Acetobacterium woodii ATP synthase, at 2.1 Å resolution. Unlike known structures, this rotor ring is a 9:1 heteromer of F- and V-type c-subunits and therefore features a hybrid configuration of ion-binding sites along its circumference. Molecular and kinetic simulations are used to dissect the mechanisms of Na(+) recognition and rotation of this c-ring, and to explain the functional implications of the V-type c-subunit. These structural and mechanistic insights indicate an evolutionary path between synthases and pumps involving adaptations in the rotor ring.

Indexed as

AcetobacteriumAdenosine DiphosphateAdenosine TriphosphateATP Synthetase ComplexesCrystallizationHydrogenMicroscopy, Atomic ForceModels, BiologicalMolecular Dynamics SimulationProtein SubunitsSodiumAdenosine DiphosphateAdenosine TriphosphateATP Synthetase ComplexesHydrogenProtein SubunitsSodium

Identifiers

PMID25381992
PMCPMC4228694
OpenAlexW2061901010

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.