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

Tijdschriftbijdrage - Tijdschriftartikel

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.

Tijdschrift: Cell (Cambridge)
ISSN: 0092-8674
Issue: 3
Volume: 176
Pagina's: 435-447.e15
Jaar van publicatie:2019
Trefwoorden:adenine nucleotide translocase, adenine nucleotide translocator, alternating access mechanism, bioenergetics, bongkrekate, cardiolipin, induced fit, mitochondria, transport mechanism
  • PubMed Central Id: PMC6349463
  • DOI: https://doi.org/10.1016/j.cell.2018.11.025
  • ORCID: /0000-0003-0454-4227/work/53935397
  • Scopus Id: 85060144527
  • ORCID: /0000-0002-3825-874X/work/61109781
  • ORCID: /0000-0002-2466-0172/work/62063049
  • WoS Id: 000456526100006
CSS-citation score:4
Toegankelijkheid:Open