Evidence map›Paper›PMID 26167881›Full record

ArticleNature structural & molecular biology2015

Substrate-modulated ADP/ATP-transporter dynamics revealed by NMR relaxation dispersion.

Sven Brüschweiler, Qin Yang, Changqing Run, James J Chou

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 53 citations in OpenAlex.

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  6. Molecular Dynamics Simulations of Mitochondrial Uncoupling Protein 2.International journal of molecular sciences · 2021
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  15. The Journal of biological chemistry · 2018
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Sven BrüschweilerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
Qin YangDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
Changqing Run1] National Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China. [2] State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China.
James J Chou1] Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA. [2] National Center for Protein Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China. [3] State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China.
Chinese Academy of Sciences · CNHarvard University · US

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2014
$11.5M
AvanceIII 700MHz NMR spectrometer with cryogenic probeS10RR029236 · NCRR · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2010
$1.6M
NCRR NIH HHS S10 RR029236NIBIB NIH HHS P41 EB-002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM094608NIGMS NIH HHS U54 GM094608
6 · The paper itself

Abstract

The ADP/ATP carrier (AAC) transports ADP and ATP across the inner mitochondrial membrane. Unlike most transporters, which have two-fold direct or inverted quasisymmetry, AAC has apparent three-fold rotational symmetry. Further, its transport rate is relatively fast for transporters that carry large solutes. Here, we study the yeast AAC carrier 3 by obtaining comprehensive NMR relaxation dispersion measurements, which provide residue-specific information on the protein's conformational exchange. Our data indicate that AAC is predominantly in the cytosol-facing open state and converts to a sparsely populated state in an asymmetric manner despite its three-fold structural symmetry. Binding of the substrate ADP substantially increases the rate of conformational exchange, whereas the inhibitor CATR slows the exchange. These results suggest that although the transporter catalyzes the translocation of substrate the substrate also facilitates interconversion between alternating states, and this interconversion may be relevant to the transport function.

Indexed as

Protein Structure, SecondaryProtein Structure, TertiaryAdenosine DiphosphateAlgorithmsBinding SitesKineticsMagnetic Resonance SpectroscopyMitochondrial ADP, ATP TranslocasesModels, MolecularProtein BindingProtein ConformationSaccharomyces cerevisiae ProteinsSubstrate SpecificityThermodynamicsAdenosine DiphosphateMitochondrial ADP, ATP TranslocasesSaccharomyces cerevisiae Proteins

Identifiers

PMID26167881
PMCPMC4527935
OpenAlexW2224543239

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.