Copper chaperones: function, structure and copper-binding properties.

摘要: Copper is an absolute requirement for living systems and the intracellular trafficking of this metal to copper-dependent proteins fundamental normal cellular metabolism. The copper chaperones perform dual functions prevention cytoplasmic exposure ions in transit. Only a small number have been identified at time but their conservation across plant, bacterial animal species suggests that majority utilise these routing. available data suggest each protein cell served by specific chaperone. Although cannot be substituted one another given type, deliver same different types appear functionally equivalent. thus far "open-faced β-sandwich" global fold with conserved MXCXXC metal-binding motif. Specificity appears mediated residues surrounding copper-binding binds such as Cu(I) trigonal complex three sulfur ligands. chaperone cytochrome-c-oxidase, Cox17, deviates from design.