2GGP
Solution structure of the Atx1-Cu(I)-Ccc2a complex
Summary for 2GGP
| Entry DOI | 10.2210/pdb2ggp/pdb |
| Descriptor | Metal homeostasis factor ATX1, Probable copper-transporting ATPase, COPPER (I) ION (3 entities in total) |
| Functional Keywords | copper transport, complex, structural genomics, structural proteomics in europe, spine, chaperone, metal transport |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Cytoplasm: P38636 Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein: P38995 |
| Total number of polymer chains | 2 |
| Total formula weight | 16186.12 |
| Authors | Banci, L.,Bertini, I.,Cantini, F.,Felli, I.C.,Gonnelli, L.,Hadjiliadis, N.,Pierattelli, R.,Rosato, A.,Voulgaris, P.,Structural Proteomics in Europe (SPINE) (deposition date: 2006-03-24, release date: 2006-08-08, Last modification date: 2024-05-29) |
| Primary citation | Banci, L.,Bertini, I.,Cantini, F.,Felli, I.C.,Gonnelli, L.,Hadjiliadis, N.,Pierattelli, R.,Rosato, A.,Voulgaris, P. The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction. Nat.Chem.Biol., 2:367-368, 2006 Cited by PubMed Abstract: Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, we structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase. Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners. PubMed: 16732294DOI: 10.1038/nchembio797 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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