2G9O
Solution structure of the apo form of the third metal-binding domain of ATP7A protein (Menkes Disease protein)
Summary for 2G9O
| Entry DOI | 10.2210/pdb2g9o/pdb |
| Related | 2GA7 |
| NMR Information | BMRB: 7069 |
| Descriptor | Copper-transporting ATPase 1 (1 entity in total) |
| Functional Keywords | menkes disease, solution structure, structural genomics, structural proteomics in europe, spine, hydrolase |
| 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 | 9873.03 |
| Authors | Banci, L.,Bertini, I.,Cantini, F.,DellaMalva, N.,Rosato, A.,Herrmann, T.,Wuthrich, K.,Structural Proteomics in Europe (SPINE) (deposition date: 2006-03-07, release date: 2006-08-01, Last modification date: 2024-05-29) |
| Primary citation | Banci, L.,Bertini, I.,Cantini, F.,DellaMalva, N.,Herrmann, T.,Rosato, A.,Wuthrich, K. Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein. J.Biol.Chem., 281:29141-29147, 2006 Cited by PubMed Abstract: The third metal-binding domain of the human Menkes protein (MNK3), a copper(I)-transporting ATPase, has been expressed in Escherichia coli and characterized in solution. The solution structure of MNK3, its copper(I)-binding properties, and its interaction with the physiological partner, HAH1, have been studied. MNK3 is the domain most dissimilar in structure from the other domains of the Menkes protein. This is reflected in a significant rearrangement of the last strand of the four-stranded beta-sheet when compared with the other known homologous proteins or protein domains. MNK3 is also peculiar with respect to its interaction with the copper(I) ion, as it was found to be a comparatively weak binder. Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains. PubMed: 16873374DOI: 10.1074/jbc.M603176200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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