Evidence map›Paper›PMID 20173764›Full record

ArticleNature structural & molecular biology2010

The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase.

Lawrence K Lee, Alastair G Stewart, Mhairi Donohoe, Ricardo A Bernal, Daniela Stock

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. 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
7.2field-weighted citation impact, top 2% 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, 91 citations in OpenAlex.

  1. The ATP Synthase SubunitsInternational journal of molecular sciences · 2023
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019
    Review
  8. Article
  9. Cryo EM structure of intact rotary HNature communications · 2018
    Article
  10. The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

5 authors at 2 institutions in 2 countries.

Lawrence K LeeStructural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.
Alastair G Stewart
Mhairi Donohoe
Ricardo A Bernal
Daniela Stock
Victor Chang Cardiac Research Institute · AUThe University of Texas at El Paso · US

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI YANG, XIANGZHONG · 2002 to 2011
$17.3M
Medical Research Council MC_U105170645NCI NIH HHS Y1-CO-1020NCRR NIH HHS P41 RR007707NCRR NIH HHS RR007707NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Proton-translocating ATPases are ubiquitous protein complexes that couple ATP catalysis with proton translocation via a rotary catalytic mechanism. The peripheral stalks are essential components that counteract torque generated from proton translocation during ATP synthesis or from ATP hydrolysis during proton pumping. Despite their essential role, the peripheral stalks are the least conserved component of the complexes, differing substantially between subtypes in composition and stoichiometry. We have determined the crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus consisting of subunits E and G. The structure contains a heterodimeric right-handed coiled coil, a protein fold never observed before. We have fitted this structure into the 23 A resolution EM density of the intact A-ATPase complex, revealing the precise location of the peripheral stalk and new implications for the function and assembly of proton-translocating ATPases.

Indexed as

Models, MolecularAmino Acid SequenceCrystallography, X-RayMolecular Sequence DataProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProton-Translocating ATPasesThermus thermophilusProton-Translocating ATPases

Identifiers

PMID20173764
PMCPMC2912985
OpenAlexW2055464120

What OpenQuestion holds

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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.