Structure and chemistry of the copper chaperone proteins.
Major advances have been made in the past year towards an understanding of the structure and chemistry of copper chaperone proteins. Three-dimensional structures of Atx1, CopZ, yCCS, and hCCSdII were determined, and reveal a remarkable structural similarity between chaperones and target proteins. In addition, biochemical studies of CCS suggested that chaperones are required in vivo because intracellular copper concentrations are extremely low and also indicated that copper transfer occurs via a direct protein-protein interaction.
Rosenzweig
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Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA. amyr@nwu.edu
O'Halloran
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D000595:Amino Acid Sequence; D000818:Animals; D003300:Copper; D006801:Humans; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013482:Superoxide Dismutase / Q000737:chemistry
D008667:Metalloproteins; D018832:Molecular Chaperones; D003300:Copper; D013482:Superoxide Dismutase