Nucleotide exchange in mitochondria: insight at a molecular level.
Mitochondrial carrier proteins are embedded in the inner mitochondrial membrane and ensure the transport of many important metabolites. The ADP/ATP carrier imports ADP into the mitochondrial matrix in exchange for ATP after synthesis. It is the most studied mitochondrial carrier and its structure was the first to be unraveled at high resolution. The structure reveals six transmembrane helices forming a tightly closed bundle toward the matrix and a funnel-shaped cavity opening toward the intermembrane space. The cavity ends in a narrow pit 10A from the matrix. The analysis of residues located in the cavity hints at the mechanism of binding of adenine nucleotides. Additionally, the presence of conserved proline residues in three sharply kinked helices suggests a translocation mechanism.
Institut de Biologie Structurale, UMR 5075 CEA-CNRS-Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble cedex 1, France. pebay@ibs.fr
Eva
E
Pebay-Peyroula
Gérard
G
Brandolin
D019281:Dimerization; D008928:Mitochondria / Q000378:metabolism*; D000226:Mitochondrial ADP, ATP Translocases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D009711:Nucleotides; D000226:Mitochondrial ADP, ATP Translocases