1OKC

structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside

Summary for 1OKC

• Entry DOI: 10.2210/pdb1okc/pdb
• Descriptor: ADP, ATP CARRIER PROTEIN HEART ISOFORM T1, Carboxyatractyloside, CARDIOLIPIN, ... (6 entities in total)
• Functional Keywords: mitochondrial transporter, nucleotide translocation, membrane protein, carrier protein, transport protein
• Biological source: BOS TAURUS (CATTLE)
• Cellular location: Mitochondrion inner membrane; Multi-pass membrane protein: P02722
• Total number of polymer chains: 1
• Total formula weight: 41803.73

Authors

Pebay-Peyroula, E.,Dahout-Gonzalez, C.,Kahn, R.,Trezeguet, V.,Lauquin, G.J.-M.,Brandolin, G. (deposition date: 2003-07-21, release date: 2003-11-07, Last modification date: 2024-05-08)

Primary citation

Pebay-Peyroula, E.,Dahout-Gonzalez, C.,Kahn, R.,Trezeguet, V.,Lauquin, G.J.-M.,Brandolin, G.
Structure of Mitochondrial Adp/ATP Carrier in Complex with Carboxyatractyloside
Nature, 426:39-, 2003

PubMed 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 A by X-ray crystallography in complex with an inhibitor, carboxyatractyloside. Six alpha-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.

PubMed: 14603310
DOI: 10.1038/NATURE02056

Experimental method

X-RAY DIFFRACTION (2.2 Å)