Evidence map›Paper›PMID 30611538›Full record

ArticleCell2019

The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.

Jonathan J Ruprecht, Martin S King, Thomas Zögg, Antoniya A Aleksandrova, Els Pardon, Paul G Crichton, Jan Steyaert, Edmund R S Kunji

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 199 papers.

0numbers the graph read from it
0cells of the map it votes in
199citing papers in PubMed
14.5field-weighted citation impact, top 1% 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

199 citing papers in PubMed, 310 citations in OpenAlex.

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  18. Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026
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  20. Review

139 more citing papers are in PubMed but not listed here.

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 4 institutions in 3 countries.

Jonathan J RuprechtMRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK. Electronic address: jjr@mrc-mbu.cam.ac.uk.
Martin S KingMRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.
Thomas ZöggVIB-VUB Center for Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
Antoniya A AleksandrovaComputational Structural Biology Section, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD 20892, USA.
Els PardonVIB-VUB Center for Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
Paul G CrichtonMRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.
Jan SteyaertVIB-VUB Center for Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
Edmund R S KunjiMRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK. Electronic address: ek@mrc-mbu.cam.ac.uk.
University of Cambridge · GBVIB-VUB Center for Structural Biology · BEMRC Mitochondrial Biology Unit · GBNational Institute of Neurological Disorders and Stroke · US

Funding

Medical Research Council MC_UU_00015/1
6 · The paper itself

Abstract

Mitochondrial ADP/ATP carriers transport ADP into the mitochondrial matrix for ATP synthesis, and ATP out to fuel the cell, by cycling between cytoplasmic-open and matrix-open states. The structure of the cytoplasmic-open state is known, but it has proved difficult to understand the transport mechanism in the absence of a structure in the matrix-open state. Here, we describe the structure of the matrix-open state locked by bongkrekic acid bound in the ADP/ATP-binding site at the bottom of the central cavity. The cytoplasmic side of the carrier is closed by conserved hydrophobic residues, and a salt bridge network, braced by tyrosines. Glycine and small amino acid residues allow close-packing of helices on the matrix side. Uniquely, the carrier switches between states by rotation of its three domains about a fulcrum provided by the substrate-binding site. Because these features are highly conserved, this mechanism is likely to apply to the whole mitochondrial carrier family. VIDEO ABSTRACT.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceBinding SitesBiological TransportBongkrekic AcidCytoplasmMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsModels, MolecularProtein ConformationProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine DiphosphateAdenosine TriphosphateBongkrekic AcidMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsSaccharomyces cerevisiae Proteinsadenine nucleotide translocaseadenine nucleotide translocatoralternating access mechanismbioenergeticsbongkrekatecardiolipininduced fitmitochondriatransport mechanism

Identifiers

PMID30611538
PMCPMC6349463
OpenAlexW2907890950

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.