Ontology highlight
ABSTRACT:
SUBMITTER: Banci L
PROVIDER: S-EPMC3190761 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Banci Lucia L Bertini Ivano I Cefaro Chiara C Ciofi-Baffoni Simone S Gallo Angelo A
The Journal of biological chemistry 20110804 39
Human Cox17 is the mitochondrial copper chaperone responsible for supplying copper ions, through the assistance of Sco1, Sco2, and Cox11, to cytochrome c oxidase, the terminal enzyme of the mitochondrial energy-transducing respiratory chain. It consists of a coiled coil-helix-coiled coil-helix domain stabilized by two disulfide bonds and binds one copper(I) ion through a Cys-Cys motif. Here, the structures and the backbone mobilities of two Cox17 mutated forms with only one interhelical disulfid ...[more]