Evidence map›Paper›PMID 32879423›Full record

ArticleCommunications biology2020

Structural basis of redox modulation on chloroplast ATP synthase.

Jay-How Yang, Dewight Williams, Eaazhisai Kandiah, Petra Fromme, Po-Lin Chiu

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Biochemistry · 2026
    Article
  5. Review
  6. Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. The chloroplast ATP synthase redox domain inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Directed proton transfer from FBiophysical reviews · 2023
    Review
  13. FInternational journal of molecular sciences · 2023
    Review
  14. Two specific domains of the γ subunit of chloroplast FProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. ATP synthase FCellular and molecular life sciences : CMLS · 2022
    Review
  20. Recent Advances inJournal of fungi (Basel, Switzerland) · 2022
    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

5 authors at 2 institutions in 2 countries.

Jay-How YangCenter for Applied Structural Discovery (CASD), Biodesign Institute, Arizona State University, Tempe, AZ, USA.
Dewight WilliamsEyring Materials Center, Arizona State University, Tempe, AZ, 85287, USA.
Eaazhisai KandiahEuropean Synchrotron Radiation Facility, 38000, Grenoble, France.
Petra FrommeCenter for Applied Structural Discovery (CASD), Biodesign Institute, Arizona State University, Tempe, AZ, USA. Petra.Fromme@asu.edu.
Po-Lin ChiuCenter for Applied Structural Discovery (CASD), Biodesign Institute, Arizona State University, Tempe, AZ, USA. plchiu@asu.edu.ORCID http://orcid.org/0000-0001-8608-7650
Arizona State University · USEuropean Synchrotron Radiation Facility · FR

Funding

Structure and Function of the proton-turbine of the ATP-SynthaseR01GM081490 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2007 to 2010
$1.0M
NIGMS NIH HHS R01 GM081490
6 · The paper itself

Abstract

In higher plants, chloroplast ATP synthase has a unique redox switch on its γ subunit that modulates enzyme activity to limit ATP hydrolysis at night. To understand the molecular details of the redox modulation, we used single-particle cryo-EM to determine the structures of spinach chloroplast ATP synthase in both reduced and oxidized states. The disulfide linkage of the oxidized γ subunit introduces a torsional constraint to stabilize the two β hairpin structures. Once reduced, free cysteines alleviate this constraint, resulting in a concerted motion of the enzyme complex and a smooth transition between rotary states to facilitate the ATP synthesis. We added an uncompetitive inhibitor, tentoxin, in the reduced sample to limit the flexibility of the enzyme and obtained high-resolution details. Our cryo-EM structures provide mechanistic insight into the redox modulation of the energy regulation activity of chloroplast ATP synthase.

Indexed as

BiocatalysisChloroplast Proton-Translocating ATPasesCryoelectron MicroscopyLightModels, BiologicalModels, MolecularNucleotidesOxidation-ReductionProtein DomainsProtein SubunitsSpinacia oleraceaStatistics as TopicStructure-Activity RelationshipChloroplast Proton-Translocating ATPasesNucleotidesProtein Subunits

Identifiers

PMID32879423
PMCPMC7468127
OpenAlexW3081705730

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.