Evidence map›Paper›PMID 31251901›Full record

ArticleBiochimica et biophysica acta. Bioenergetics2019

Interaction between γC87 and γR242 residues participates in energy coupling between catalysis and proton translocation in Escherichia coli ATP synthase.

Yunxiang Li, Xinyou Ma, Joachim Weber

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Bioenergetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 2 institutions in 1 country.

Yunxiang LiDepartment of Chemistry and Biochemistry, Texas Woman's University, Denton, TX 76204, USA; Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USA. Electronic address: yli7@twu.edu.
Xinyou MaDepartment of Chemistry, The University of Chicago, Chicago, IL 60637, USA.
Joachim WeberDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USA; The Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Texas Tech University · USUniversity of Chicago · US

Funding

Catalytic mechanism of F1Fo-ATP synthaseR01GM071462 · NIGMS · TEXAS TECH UNIVERSITY · PI WEBER, JOACHIM · 2004 to 2010
$1.2M
NIGMS NIH HHS R01 GM071462
6 · The paper itself

Abstract

Functioning as a nanomotor, ATP synthase plays a vital role in the cellular energy metabolism. Interactions at the rotor and stator interface are critical to the energy transmission in ATP synthase. From mutational studies, we found that the γC87K mutation impairs energy coupling between proton translocation and nucleotide synthesis/hydrolysis. An additional glutamine mutation at γR242 (γR242Q) can restore efficient energy coupling to the γC87K mutant. Arrhenius plots and molecular dynamics simulations suggest that an extra hydrogen bond could form between the side chains of γC87K and β

Indexed as

Amino AcidsBiocatalysisEnergy MetabolismEscherichia coliEscherichia coli ProteinsHydrogen BondingMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein SubunitsProton-Translocating ATPasesAmino AcidsEscherichia coli ProteinsProtein SubunitsProton-Translocating ATPasesATP synthaseEnergy transmissionMolecular dynamicsMutational studyResidue interaction

Identifiers

PMID31251901
PMCPMC6668360
OpenAlexW2954484247

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.