title: P-type ATPases.
abstract: P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by these biological nanomachines. Phylogenetically, P-type ATPases are divided into five subfamilies, P1-P5. These subfamilies differ with respect to transported ligands and the way they are regulated.
authors.affiliation: Center for Membrane Pumps in Cells and Disease--PUMPKIN, Danish National Research Foundation, University of Copenhagen, Frederiksberg C, Denmark. palmgren@life.ku.dk
authors.forename: Michael G
authors.initials: MG
authors.lastname: Palmgren
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D003198:Computer Simulation; D015640:Ion Channel Gating / Q000502:physiology*; D050356:Lipid Metabolism / Q000502:physiology*; D008055:Lipids / Q000737:chemistry*; D008954:Models, Biological; D008956:Models, Chemical; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D008055:Lipids; D000251:Adenosine Triphosphatases