1Q8L
Second Metal Binding Domain of the Menkes ATPase
Summary for 1Q8L
| Entry DOI | 10.2210/pdb1q8l/pdb |
| Related | 1AW0 |
| NMR Information | BMRB: 6022 |
| Descriptor | Copper-transporting ATPase 1 (1 entity in total) |
| Functional Keywords | metal binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Isoform 3: Cytoplasm, cytosol (Probable). Isoform 5: Endoplasmic reticulum: Q04656 |
| Total number of polymer chains | 1 |
| Total formula weight | 9309.01 |
| Authors | Jones, C.E.,Daly, N.L.,Cobine, P.A.,Craik, D.J.,Dameron, C.T. (deposition date: 2003-08-21, release date: 2004-01-20, Last modification date: 2024-05-22) |
| Primary citation | Jones, C.E.,Daly, N.L.,Cobine, P.A.,Craik, D.J.,Dameron, C.T. Structure and metal binding studies of the second copper binding domain of the Menkes ATPase. J.Struct.Biol., 143:209-218, 2003 Cited by PubMed Abstract: Biological utilisation of copper requires that the metal, in its ionic forms, be meticulously transported, inserted into enzymes and regulatory proteins, and excess be excreted. To understand the trafficking process, it is crucial that the structures of the proteins involved in the varied processes be resolved. To investigate copper binding to a family of structurally related copper-binding proteins, we have characterised the second Menkes N-terminal domain (MNKr2). The structure, determined using 1H and 15N heteronuclear NMR, of the reduced form of MNKr2 has revealed two alpha-helices lying over a single beta-sheet and shows that the binding site, a Cys(X)2Cys pair, is located on an exposed loop. 1H-15N HSQC experiments demonstrate that binding of Cu(I) causes changes that are localised to conserved residues adjacent to the metal binding site. Residues in this area are important to the delivery of copper by the structurally related Cu(I) chaperones. Complementary site-directed mutagenesis of the adjacent residues has been used to probe the structural roles of conserved residues. PubMed: 14572476DOI: 10.1016/j.jsb.2003.08.008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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