Title : COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase.

Pub. Date : 2019 Dec 17

PMID : 31851937






4 Functional Relationships(s)
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1 Insertion of copper into its catalytically active subunits, including COX2, is a complex process that requires metallochaperones and redox proteins including SCO1, SCO2, and COA6, a recently discovered protein whose molecular function is unknown. Copper mitochondrially encoded cytochrome c oxidase II Homo sapiens
2 To uncover the molecular mechanism by which COA6 and SCO proteins mediate copper delivery to COX2, we have solved the solution structure of COA6, which reveals a coiled-coil-helix-coiled-coil-helix domain typical of redox-active proteins found in the mitochondrial inter-membrane space. Copper mitochondrially encoded cytochrome c oxidase II Homo sapiens
3 Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Copper mitochondrially encoded cytochrome c oxidase II Homo sapiens
4 Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding. Copper mitochondrially encoded cytochrome c oxidase II Homo sapiens