6PCE
Human Coa6
Summary for 6PCE
| Entry DOI | 10.2210/pdb6pce/pdb |
| Descriptor | Cytochrome c oxidase assembly factor 6 homolog, SULFATE ION (3 entities in total) |
| Functional Keywords | coa6 copper cytochrome c oxidase mitochondria structure, metal binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 17197.32 |
| Authors | Maher, M.J.,Maghool, S. (deposition date: 2019-06-17, release date: 2019-10-02, Last modification date: 2024-11-20) |
| Primary citation | Maghool, S.,Cooray, N.D.G.,Stroud, D.A.,Aragao, D.,Ryan, M.T.,Maher, M.J. Structural and functional characterization of the mitochondrial complex IV assembly factor Coa6. Life Sci Alliance, 2:-, 2019 Cited by PubMed Abstract: Assembly factors play key roles in the biogenesis of many multi-subunit protein complexes regulating their stability, activity, and the incorporation of essential cofactors. The human assembly factor Coa6 participates in the biogenesis of the Cu site in complex IV (cytochrome oxidase, COX). Patients with mutations in Coa6 suffer from mitochondrial disease due to complex IV deficiency. Here, we present the crystal structures of human Coa6 and the pathogenic Coa6-mutant protein. These structures show that Coa6 has a 3-helical bundle structure, with the first 2 helices tethered by disulfide bonds, one of which likely provides the copper-binding site. Disulfide-mediated oligomerization of the Coa6 protein provides a structural explanation for the loss-of-function mutation. PubMed: 31515291DOI: 10.26508/lsa.201900458 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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