Evidence map›Paper›PMID 22628564›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Engineering rotor ring stoichiometries in the ATP synthase.

Denys Pogoryelov, Adriana L Klyszejko, Ganna O Krasnoselska, Eva-Maria Heller, Vanessa Leone, Julian D Langer, Janet Vonck, Daniel J Müller, José D Faraldo-Gómez, Thomas Meier

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 90 citations in OpenAlex.

  1. ATP synthesis driven by atmospheric hydrogen concentrations.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. ATP synthase FCellular and molecular life sciences : CMLS · 2022
    Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Unusual features of the c-ring of FScientific reports · 2019
    Article
  15. Article
  16. Mechanisms for achieving high speed and efficiency in biomolecular machines.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Heterocyst Thylakoid Bioenergetics.Life (Basel, Switzerland) · 2019
    Review
  18. Article
  19. Article
  20. The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018
    Review
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

10 authors at 4 institutions in 3 countries.

Denys PogoryelovDepartment of Structural Biology, Max-Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany. denys.pogoryelov@biophys.mpg.de
Adriana L Klyszejko
Ganna O Krasnoselska
Eva-Maria Heller
Vanessa Leone
Julian D Langer
Janet Vonck
Daniel J Müller
José D Faraldo-Gómez
Thomas Meier
Max Planck Institute of Biophysics · DEMax Planck Society · DEÉcole Polytechnique Fédérale de Lausanne · CHInstitute of Molecular Biology and Biophysics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP synthase membrane rotors consist of a ring of c-subunits whose stoichiometry is constant for a given species but variable across different ones. We investigated the importance of c/c-subunit contacts by site-directed mutagenesis of a conserved stretch of glycines (GxGxGxGxG) in a bacterial c(11) ring. Structural and biochemical studies show a direct, specific influence on the c-subunit stoichiometry, revealing c(<11), c(12), c(13), c(14), and c(>14) rings. Molecular dynamics simulations rationalize this effect in terms of the energetics and geometry of the c-subunit interfaces. Quantitative data from a spectroscopic interaction study demonstrate that the complex assembly is independent of the c-ring size. Real-time ATP synthesis experiments in proteoliposomes show the mutant enzyme, harboring the larger c(12) instead of c(11), is functional at lower ion motive force. The high degree of compliance in the architecture of the ATP synthase rotor offers a rationale for the natural diversity of c-ring stoichiometries, which likely reflect adaptations to specific bioenergetic demands. These results provide the basis for bioengineering ATP synthases with customized ion-to-ATP ratios, by sequence modifications.

Indexed as

Adenosine TriphosphateATP Synthetase ComplexesElectrophoresis, Polyacrylamide GelMicroscopy, Atomic ForceMicroscopy, ElectronModels, MolecularMutationProtein ConformationProteolipidsSurface Plasmon ResonanceAdenosine TriphosphateATP Synthetase ComplexesProteolipidsproteoliposomes

Identifiers

PMID22628564
PMCPMC3382517
OpenAlexW2081470321

What OpenQuestion holds

Textmetadata
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.