Copper delivery by metallochaperone proteins.
Copper is an essential element in all living organisms, serving as a cofactor for many important proteins and enzymes. Metallochaperone proteins deliver copper ions to specific physiological partners by direct protein-protein interactions. The Atx1-like chaperones transfer copper to intracellular copper transporters, and the CCS chaperones shuttle copper to copper,zinc superoxide dismutase. Crystallographic studies of these two copper chaperone families have provided insights into metal binding and target recognition by metallochaperones and have led to detailed molecular models for the copper transfer mechanism.
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Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois 60208, USA. amyr@northwestern.edu
D002352:Carrier Proteins; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D011485:Protein Binding; D029701:Saccharomyces cerevisiae Proteins; D013482:Superoxide Dismutase / Q000378:metabolism
C093341:ATX1 protein, S cerevisiae; C491960:CCS1 protein, S cerevisiae; D002352:Carrier Proteins; D005656:Fungal Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D013482:Superoxide Dismutase