1Z2G
Solution structure of apo, oxidized yeast Cox17
Summary for 1Z2G
| Entry DOI | 10.2210/pdb1z2g/pdb |
| Related | 1U96 1U97 |
| Descriptor | Cytochrome c oxidase copper chaperone (1 entity in total) |
| Functional Keywords | copper chaperone, cytochrome c oxidase assembly, disulfide bonds, coiled coil-helix-coiled coil-helix domain, structural genomics, structural proteomics in europe, spine, chaperone |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Mitochondrion intermembrane space: Q12287 |
| Total number of polymer chains | 1 |
| Total formula weight | 8069.09 |
| Authors | Arnesano, F.,Balatri, E.,Banci, L.,Bertini, I.,Winge, D.R.,Structural Proteomics in Europe (SPINE) (deposition date: 2005-03-08, release date: 2005-06-07, Last modification date: 2024-10-30) |
| Primary citation | Arnesano, F.,Balatri, E.,Banci, L.,Bertini, I.,Winge, D.R. Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding STRUCTURE, 13:713-722, 2005 Cited by PubMed Abstract: Cox17 is a key mitochondrial copper chaperone involved in the assembly of cytochrome c oxidase (COX). The NMR solution structure of the oxidized apoCox17 isoform consists of a coiled-coil conformation stabilized by two disulfide bonds involving Cys(26)/Cys(57) and Cys(36)/Cys(47). This appears to be a conserved tertiary fold of a class of proteins, localized within the mitochondrial intermembrane space, that contain a twin Cys-x(9)-Cys sequence motif. An isomerization of one disulfide bond from Cys(26)/Cys(57) to Cys(24)/Cys(57) is required prior to Cu(I) binding to form the Cu(1)Cox17 complex. Upon further oxidation of the apo-protein, a form with three disulfide bonds is obtained. The reduction of all disulfide bonds provides a molten globule form that can convert to an additional conformer capable of binding up to four Cu(I) ions in a polycopper cluster. This form of the protein is oligomeric. These properties are framed within a complete model of mitochondrial import and COX assembly. PubMed: 15893662DOI: 10.1016/j.str.2005.02.015 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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