The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier.
Cell
; 176(3): 435-447.e15, 2019 01 24.
Article
em En
| MEDLINE
| ID: mdl-30611538
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Translocases Mitocondriais de ADP e ATP
/
Mitocôndrias
Idioma:
En
Revista:
Cell
Ano de publicação:
2019
Tipo de documento:
Article