ATP7A

1AW0, 1KVI, 1KVJ, 1Q8L, 1S6O, 1S6U, 1Y3J, 1Y3K, 1YJR, 1YJT, 1YJU, 1YJV, 2G9O, 2GA7, 2K1R, 2KIJ, 2KMV, 2KMX, 3CJK53811977ENSG00000165240ENSMUSG00000033792Q04656Q64430NM_000052NM_001282224NM_001109757NM_009726NP_000043NP_001269153NP_001103227NP_033856ATP7A, also known as Menkes' protein (MNK), is a copper-transporting P-type ATPase which uses the energy arising from ATP hydrolysis to transport Cu(I) across cell membranes. The ATP7A protein is a transmembrane protein and is expressed in the intestine and all tissues except liver. In the intestine, ATP7A regulates Cu(I) absorption in the human body by transporting Cu(I) from the small intestine into the blood. In other tissues, ATP7A shuttles between the Golgi apparatus and the cell membrane to maintain proper Cu(I) concentrations (since there is no free Cu(I) in the cell, Cu(I) ions are all tightly bound) in the cell and provides certain enzymes with Cu(I) (e.g. peptidyl-α-monooxygenase, tyrosinase, and lysyl oxidase). The X-linked, inherited, lethal genetic disorder of the ATP7A gene causes Menkes disease, a copper deficiency resulting in early childhood death.1aw0: FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES1kvi: Solution Structure of the Reduced Form of the First Heavy Metal Binding Motif of the Menkes Protein1kvj: Solution Structure of the Cu(I) bound form of the first heavy metal binding motif of the Menkes protein1q8l: Second Metal Binding Domain of the Menkes ATPase1s6o: Solution structure and backbone dynamics of the apo-form of the second metal-binding domain of the Menkes protein ATP7A1s6u: Solution structure and backbone dynamics of the Cu(I) form of the second metal-binding domain of the Menkes protein ATP7A1y3j: Solution structure of the copper(I) form of the fifth domain of Menkes protein1y3k: Solution structure of the apo form of the fifth domain of Menkes protein1yjr: Solution structure of the apo form of the sixth soluble domain A69P mutant of Menkes protein1yjt: Solution structure of the Cu(I) form of the sixth soluble domain A69P mutant of Menkes protein1yju: Solution structure of the apo form of the sixth soluble domain of Menkes protein1yjv: Solution structure of the Cu(I) form of the sixth soluble domain of Menkes protein2aw0: FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES2g9o: Solution structure of the apo form of the third metal-binding domain of ATP7A protein (Menkes Disease protein)2ga7: Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein) ATP7A, also known as Menkes' protein (MNK), is a copper-transporting P-type ATPase which uses the energy arising from ATP hydrolysis to transport Cu(I) across cell membranes. The ATP7A protein is a transmembrane protein and is expressed in the intestine and all tissues except liver. In the intestine, ATP7A regulates Cu(I) absorption in the human body by transporting Cu(I) from the small intestine into the blood. In other tissues, ATP7A shuttles between the Golgi apparatus and the cell membrane to maintain proper Cu(I) concentrations (since there is no free Cu(I) in the cell, Cu(I) ions are all tightly bound) in the cell and provides certain enzymes with Cu(I) (e.g. peptidyl-α-monooxygenase, tyrosinase, and lysyl oxidase). The X-linked, inherited, lethal genetic disorder of the ATP7A gene causes Menkes disease, a copper deficiency resulting in early childhood death. The ATP7A gene is located on the long (q) arm of the X chromosome at band Xq21.1. The encoded ATP7A protein has 1,500 amino acids. Mutations/additions/deletions of this gene often cause copper deficiency, which leads to progressive neurodegeneration and death in children. ATP7A is a transmembrane protein with the N- and C-termini both oriented towards the cytosol (see picture). It is highly homologous to protein ATP7B. ATP7A contains three major functional domains: Many motifs in the ATP7A structure are conserved: