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ATP–ADP translocase : ウィキペディア英語版 | ATP–ADP translocase
ATP–ADP translocase is a transporter protein that enables ATP and ADP to traverse the inner mitochondrial membrane. ATP produced from oxidative phosphorylation is transported from the mitochondrial matrix to the cytoplasm, whereas ADP is transported from the cytoplasm to the mitochondrial matrix. More than 10% of the protein in the inner mitochondrial membrane consists of ATP–ADP translocase. ==Structure==
ATP–ADP translocase is a protein with 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. The binding pocket, conserved throughout most isoforms, mostly consists of basic residues that allow for strong binding to ATP or ADP and has a maximal diameter of 20 Å and a depth of 30 Å. Indeed, arginine residues 96, 204, 252, 253, and 294, as well as lysine 38, have been shown to be essential for transporter activity.
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