Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside Export

@article{citeulike:3443178, 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 \r{A} by X-ray crystallography in complex with an inhibitor, carboxyatractyloside. Six -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.}, author = {Pebay-Peyroula, Eva and Dahout-Gonzalez, Cecile and Kahn, Richard and Trezeguet, Veronique and Lauquin, Guy J. M. and Brandolin, Gerard}, citeulike-article-id = {3443178}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature02056}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nature02056}, day = {06}, doi = {10.1038/nature02056}, issn = {0028-0836}, journal = {Nature}, keywords = {ant, arl, bart, effector, structure}, month = {November}, number = {6962}, pages = {39--44}, posted-at = {2008-10-23 13:01:03}, priority = {2}, publisher = {Nature Publishing Group}, title = {Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside}, url = {http://dx.doi.org/10.1038/nature02056}, volume = {426}, year = {2003} }

TY - JOUR ID - citeulike:3443178 L3 - citeulike-article-id:3443178 N2 - 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 -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. IS - 6962 JF - Nature SN - 0028-0836 EP - 44 TI - Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside PB - Nature Publishing Group VL - 426 SP - 39 KW - ant KW - arl KW - bart KW - effector KW - structure AU - Pebay-Peyroula, Eva AU - Dahout-Gonzalez, Cecile AU - Kahn, Richard AU - Trezeguet, Veronique AU - Lauquin, Guy AU - Brandolin, Gerard PY - 2003/11/06/ UR - http://dx.doi.org/10.1038/nature02056 ER -