Evidence map›Paper›PMID 26165595›Full record

ArticleStructure (London, England : 1993)2015

Molecular Basis of MgATP Selectivity of the Mitochondrial SCaMC Carrier.

Changqing Run, Qin Yang, Zhijun Liu, Bo OuYang, James J Chou

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Mechanistic insights into multiple-step transport of mitochondrial ADP/ATP carrier.Computational and structural biotechnology journal · 2022
    Article
  7. Article
  8. Review
  9. The Journal of biological chemistry · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Ion and inhibitor binding of the double-ring ion selectivity filter of the mitochondrial calcium uniporter.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation.Protein science : a publication of the Protein Society · 2016
    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 3 institutions in 2 countries.

Changqing RunNational Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China.
Qin YangDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Zhijun LiuNational Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China.
Bo OuYangNational Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China. Electronic address: ouyang@sibcb.ac.cn.
James J ChouNational Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China; State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: james_chou@hms.harvard.edu.
Chinese Academy of Sciences · CNHarvard University · USCenter for Excellence in Molecular Cell Science · CN

Funding

Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2014
$11.5M
NIGMS NIH HHS GM094608NIGMS NIH HHS U54 GM094608
6 · The paper itself

Abstract

The mitochondrial matrix is the supplier of cellular ATP. The short Ca(2+)-binding mitochondrial carrier (SCaMC) is one of the two mitochondrial carriers responsible for transporting ATP across the mitochondrial inner membrane. While the ADP/ATP carrier (AAC) accounts for the bulk ADP/ATP recycling in the matrix, the function of SCaMC is important for mitochondrial activities that depend on adenine nucleotides, such as gluconeogenesis and mitochondrial biogenesis. A key difference between SCaMC and AAC is that SCaMC selectively transports MgATP whereas AAC only transports free nucleotides. Here, we use a combination of nuclear magnetic resonance experiments and functional mutagenesis to investigate the structural basis of the MgATP selectivity in SCaMC. Our data revealed an MgATP binding site inside the transporter cavity, while identifying an aspartic acid residue that plays an important role in the higher selectivity for MgATP over free ATP.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAntiportersBinding SitesCalcium-Binding ProteinsCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionHumansMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial ProteinsModels, MolecularMolecular Sequence DataMutationAdenosine TriphosphateAntiportersCalcium-Binding ProteinsMitochondrial ADP, ATP TranslocasesMitochondrial ProteinsProteolipidsproteoliposomesRecombinant Fusion ProteinsSLC25A24 protein, human

Identifiers

PMID26165595
PMCPMC4526376
OpenAlexW1540961086

What OpenQuestion holds

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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.