title: Structure and Function of Cu(I)- and Zn(II)-ATPases.
abstract: Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.
authors.affiliation: Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University , Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
authors.forename: Oleg
authors.initials: O
authors.lastname: Sitsel
authors.affiliation: Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
authors.forename: Christina
authors.initials: C
authors.lastname: Grønberg
authors.affiliation: Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
authors.forename: Henriette Elisabeth
authors.initials: HE
authors.lastname: Autzen
authors.affiliation: Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
authors.forename: Kaituo
authors.initials: K
authors.lastname: Wang
authors.affiliation: Division of Chemistry and Chemical Engineering and Howard Hughes Medical Institute, California Institute of Technology , Pasadena, California 91125, United States.
authors.forename: Gabriele
authors.initials: G
authors.lastname: Meloni
authors.affiliation: Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University , Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
authors.affiliation: Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.|Department of Experimental Medical Science, Lund University , Sölvegatan 19, SE-221 84 Lund, Sweden.
authors.forename: Pontus
authors.initials: P
authors.lastname: Gourdon
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001692:Biological Transport; D027682:Cation Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D002413:Cations, Divalent; D002414:Cations, Monovalent; D003300:Copper / Q000378:metabolism*; D000073840:Copper-Transporting ATPases; D007501:Iron / Q000378:metabolism; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015032:Zinc / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D002413:Cations, Divalent; D002414:Cations, Monovalent; D003300:Copper; D007501:Iron; D000251:Adenosine Triphosphatases; C109898:Zn(II)-translocating P-type ATPase; D000073840:Copper-Transporting ATPases; D015032:Zinc