Perspectives in inorganic structural genomics: a trafficking route for copper

Metal ions are essential for living organisms because they are involved in many fundamental biological processes. Increasing evidence indicates that there are no free copper ions in the cell; however, a recently discovered category of proteins (metallochaperones) is responsible for copper ion trafficking and delivery to either specific target enzymes or to membrane ATPases for metal translocation. A search in the available genomes for copper chaperones and soluble domains of the ATPases reveals a large variety of systems. In this Microreview, the example of copper transfer from outside a yeast cell into the Golgi organelle is considered, as well as related processes in other eukaryotes and in prokaryotes. The investigation of the structure and metal-binding properties of these proteins is crucial for understanding the process of copper trafficking at the molecular level and how coordination chemistry may contribute to the interpretation of the energetics of the metal environment. © Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004.