Evidence map›Paper›PMID 27922000›Full record

ArticleNature communications2016

Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism.

Kun-Mou Li, Craig Wilkinson, Juho Kellosalo, Jia-Yin Tsai, Tommi Kajander, Lars J C Jeuken, Yuh-Ju Sun, Adrian Goldman

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  5. NaInternational journal of molecular sciences · 2024
    Article
  6. HParasitology research · 2024
    Review
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  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. The Mechanism of Energy Coupling in HInternational journal of molecular sciences · 2022
    Review
  15. A Lumenal Loop Associated with Catalytic Asymmetry in Plant Vacuolar HInternational journal of molecular sciences · 2021
    Article
  16. Article
  17. Catalytic Asymmetry in Homodimeric HInternational journal of molecular sciences · 2021
    Article
  18. Article
  19. Article
  20. The HFrontiers in plant science · 2020
    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

8 authors at 3 institutions in 3 countries.

Kun-Mou LiDepartment of Life Science and Institute of Bioinformatics and Structural Biology, College of Life Science, National Tsing Hua University, Hsinchu 30013, Taiwan.
Craig WilkinsonAstbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, England.
Juho KellosaloDivision of Biochemistry, Department of Biosciences, University of Helsinki, Helsinki, FIN-00014, Finland.
Jia-Yin TsaiDepartment of Life Science and Institute of Bioinformatics and Structural Biology, College of Life Science, National Tsing Hua University, Hsinchu 30013, Taiwan.
Tommi KajanderInstitute of Biotechnology, University of Helsinki, PO Box 65, Helsinki, FIN-00014, Finland.
Lars J C JeukenAstbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, England.
Yuh-Ju SunDepartment of Life Science and Institute of Bioinformatics and Structural Biology, College of Life Science, National Tsing Hua University, Hsinchu 30013, Taiwan.
Adrian GoldmanAstbury Centre for Structural Molecular Biology, School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, England.ORCID 0000-0001-8032-9700
National Tsing Hua University · TWUniversity of Leeds · GBUniversity of Helsinki · FI

Funding

European Research Council 280518
6 · The paper itself

Abstract

Membrane-bound pyrophosphatases (M-PPases), which couple proton/sodium ion transport to pyrophosphate synthesis/hydrolysis, are important in abiotic stress resistance and in the infectivity of protozoan parasites. Here, three M-PPase structures in different catalytic states show that closure of the substrate-binding pocket by helices 5-6 affects helix 13 in the dimer interface and causes helix 12 to move down. This springs a 'molecular mousetrap', repositioning a conserved aspartate and activating the nucleophilic water. Corkscrew motion at helices 6 and 16 rearranges the key ionic gate residues and leads to ion pumping. The pumped ion is above the ion gate in one of the ion-bound structures, but below it in the other. Electrometric measurements show a single-turnover event with a non-hydrolysable inhibitor, supporting our model that ion pumping precedes hydrolysis. We propose a complete catalytic cycle for both proton and sodium-pumping M-PPases, and one that also explains the basis for ion specificity.

Indexed as

BiocatalysisCell MembraneCrystallography, X-RayHydrogen BondingHydrolysisIonsKineticsModels, MolecularProtein Structure, SecondaryProton PumpsPyrophosphatasesSodiumThermotoga maritimaVignaIonsProton PumpsPyrophosphatasesSodium

Identifiers

PMID27922000
PMCPMC5150537
OpenAlexW2560010550

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.