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Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside

Author

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  • Eva Pebay-Peyroula

    (Institut de Biologie Structurale, UMR 5075 CEA-CNRS-Université Joseph Fourier)

  • Cécile Dahout-Gonzalez

    (UMR 5092 CEA-CNRS-Université Joseph Fourier, Département de Réponse et Dynamique Cellulaires, CEA-Grenoble)

  • Richard Kahn

    (Institut de Biologie Structurale, UMR 5075 CEA-CNRS-Université Joseph Fourier)

  • Véronique Trézéguet

    (Institut de Biochimie et Génétique Cellulaires)

  • Guy J.-M. Lauquin

    (Institut de Biochimie et Génétique Cellulaires)

  • Gérard Brandolin

    (UMR 5092 CEA-CNRS-Université Joseph Fourier, Département de Réponse et Dynamique Cellulaires, CEA-Grenoble)

Abstract

ATP, the principal energy currency of the cell, fuels most biosynthetic reactions in the cytoplasm by its hydrolysis into ADP and inorganic phosphate. Because resynthesis of ATP occurs in the mitochondrial matrix, ATP is exported into the cytoplasm while ADP is imported into the matrix. The exchange is accomplished by a single protein, the ADP/ATP carrier. Here we have solved the bovine carrier structure at a resolution of 2.2 Å by X-ray crystallography in complex with an inhibitor, carboxyatractyloside. Six α-helices form a compact transmembrane domain, which, at the surface towards the space between inner and outer mitochondrial membranes, reveals a deep depression. At its bottom, a hexapeptide carrying the signature of nucleotide carriers (RRRMMM) is located. Our structure, together with earlier biochemical results, suggests that transport substrates bind to the bottom of the cavity and that translocation results from a transient transition from a ‘pit’ to a ‘channel’ conformation.

Suggested Citation

  • Eva Pebay-Peyroula & Cécile Dahout-Gonzalez & Richard Kahn & Véronique Trézéguet & Guy J.-M. Lauquin & Gérard Brandolin, 2003. "Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside," Nature, Nature, vol. 426(6962), pages 39-44, November.
    • Handle: RePEc:nat:nature:v:426:y:2003:i:6962:d:10.1038_nature02056
    DOI: 10.1038/nature02056
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    Cited by:

    1. Pavel Dolezal & Michael J Dagley & Maya Kono & Peter Wolynec & Vladimir A Likić & Jung Hock Foo & Miroslava Sedinová & Jan Tachezy & Anna Bachmann & Iris Bruchhaus & Trevor Lithgow, 2010. "The Essentials of Protein Import in the Degenerate Mitochondrion of Entamoeba histolytica," PLOS Pathogens, Public Library of Science, vol. 6(3), pages 1-13, March.
    2. Antoine Gagelin & Corentin Largeau & Sandrine Masscheleyn & Mathilde S. Piel & Daniel Calderón-Mora & Frédéric Bouillaud & Jérôme Hénin & Bruno Miroux, 2023. "Molecular determinants of inhibition of UCP1-mediated respiratory uncoupling," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Vasiliki Mavridou & Martin S. King & Sotiria Tavoulari & Jonathan J. Ruprecht & Shane M. Palmer & Edmund R. S. Kunji, 2022. "Substrate binding in the mitochondrial ADP/ATP carrier is a step-wise process guiding the structural changes in the transport cycle," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Xiaojian Shi & Bryn Reinstadler & Hardik Shah & Tsz-Leung To & Katie Byrne & Luanna Summer & Sarah E. Calvo & Olga Goldberger & John G. Doench & Vamsi K. Mootha & Hongying Shen, 2022. "Combinatorial GxGxE CRISPR screen identifies SLC25A39 in mitochondrial glutathione transport linking iron homeostasis to OXPHOS," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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