2ROP
Solution structure of domains 3 and 4 of human ATP7B
Summary for 2ROP
| Entry DOI | 10.2210/pdb2rop/pdb |
| NMR Information | BMRB: 11041 |
| Descriptor | Copper-transporting ATPase 2 (1 entity in total) |
| Functional Keywords | wilson protein, mobility, protein-protein interaction, alternative splicing, atp-binding, copper, copper transport, cytoplasm, disease mutation, golgi apparatus, hydrolase, ion transport, magnesium, membrane, metal-binding, mitochondrion, nucleotide-binding, phosphoprotein, polymorphism, transmembrane, transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21143.51 |
| Authors | Banci, L.,Bertini, I.,Cantini, F.,Rosenzweig, A.C.,Yatsunyk, L.A. (deposition date: 2008-04-04, release date: 2008-10-21, Last modification date: 2024-05-15) |
| Primary citation | Banci, L.,Bertini, I.,Cantini, F.,Rosenzweig, A.C.,Yatsunyk, L.A. Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1 Biochemistry, 47:7423-7429, 2008 Cited by PubMed Abstract: The Wilson disease protein or ATP7B is a P 1B-type ATPase involved in human copper homeostasis. The extended N-terminus of ATP7B protrudes into the cytosol and contains six Cu(I) binding domains. This report presents the NMR structure of the polypeptide consisting of soluble Cu(I) binding domains 3 and 4. The two domains exhibit ferredoxin-like folds, are linked by a flexible loop, and act independently of one another. Domains 3 and 4 tend to aggregate in a concentration-dependent manner involving nonspecific intermolecular interactions. Both domains can be loaded with Cu(I) when provided as an acetonitrile complex or by the chaperone HAH1. HAH1 forms a 70% complex with domain 4 that is in fast exchange with the free protein in solution. The ability of HAH1 to form a complex only with some domains of ATP7B is an interesting property of this class of proteins and may have a signaling role in the function of the ATPases. PubMed: 18558714DOI: 10.1021/bi8004736 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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