title: Bacterial Cu(+)-ATPases: models for molecular structure-function studies.
abstract: The early discovery of the human Cu(+)-ATPases and their link to Menkes and Wilson's diseases brought attention to the unique role of these transporters in copper homeostasis. The characterization of bacterial Cu(+)-ATPases has significantly furthered our understanding of the structure, selectivity and transport mechanism of these enzymes, as well as their interplay with other elements of Cu(+) distribution networks. This review focuses on the structural-functional insights that have emerged from studies of bacterial Cu(+)-ATPases at the molecular level and how these observations have contributed to drawing up a comprehensive picture of cellular copper homeostasis.
authors.affiliation: Department of Chemistry and Biochemistry, Worcester Polytechnic Institute, 100 Institute Road, Worcester, MA 01609, USA. arguello@wpi.edu.
authors.forename: José M
authors.initials: JM
authors.lastname: Argüello
authors.forename: Sarju J
authors.initials: SJ
authors.lastname: Patel
authors.forename: Julia
authors.initials: J
authors.lastname: Quintana
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D001692:Biological Transport; D003300:Copper / Q000378:metabolism*; D000073840:Copper-Transporting ATPases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D003300:Copper; D000251:Adenosine Triphosphatases; D000073840:Copper-Transporting ATPases