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.
journal_name
Naturejournal_title
Natureauthors
Pebay-Peyroula E,Dahout-Gonzalez C,Kahn R,Trézéguet V,Lauquin GJ,Brandolin Gdoi
10.1038/nature02056keywords:
subject
Has Abstractpub_date
2003-11-06 00:00:00pages
39-44issue
6962eissn
0028-0836issn
1476-4687pii
nature02056journal_volume
426pub_type
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