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Concept
Adenine nucleotide translocator
Summary
Adenine nucleotide translocator (ANT), also known as the ADP/ATP translocase (ANT), ADP/ATP carrier protein (AAC) or mitochondrial ADP/ATP carrier, exchanges free ATP with free ADP across the inner mitochondrial membrane. ANT is the most abundant protein in the inner mitochondrial membrane and belongs to mitochondrial carrier family.
Free ADP is transported from the cytoplasm to the mitochondrial matrix, while ATP produced from oxidative phosphorylation is transported from the mitochondrial matrix to the cytoplasm, thus providing the cells with its main energy currency. ADP/ATP translocases are exclusive to eukaryotes and are thought to have evolved during eukaryogenesis. Human cells express four ADP/ATP translocases: SLC25A4, SLC25A5, SLC25A6 and SLC25A31, which constitute more than 10% of the protein in the inner mitochondrial membrane. These proteins are classified under the mitochondrial carrier superfamily.
In humans, there exist three paraologous ANT isoforms:
SLC25A4 – found primarily in heart and skeletal muscle
SLC25A5 – primarily expressed in fibroblasts
SLC25A6 – primarily express in liver
ANT has long been thought to function as a homodimer, but this concept was challenged by the projection structure of the yeast Aac3p solved by electron crystallography, which showed that the protein was three-fold symmetric and monomeric, with the translocation pathway for the substrate through the centre. The atomic structure of the bovine ANT confirmed this notion, and provided the first structural fold of a mitochondrial carrier. Further work has demonstrated that ANT is a monomer in detergents and functions as a monomer in mitochondrial membranes.
ADP/ATP translocase 1 is the major AAC in human cells and the archetypal protein of this family. It has a mass of approximately 30 kDa, consisting of 297 residues. It forms six transmembrane α-helices that form a barrel that results in a deep cone-shaped depression accessible from the outside where the substrate binds.
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