P-type ATPases

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Michael Broberg Palmgren, Københavns Universitet, Institut for Plantebiologi og Bioteknologi, Denmark
  • Poul Nissen
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.
Original languageEnglish
JournalAnnual Review of Biophysics
Pages (from-to)243-66
Number of pages24
Publication statusPublished - 2011

    Research areas

  • Adenosine Triphosphatases, Binding Sites, Computer Simulation, Ion Channel Gating, Lipid Metabolism, Lipids, Models, Biological, Models, Chemical, Protein Binding, Protein Structure, Tertiary

See relations at Aarhus University Citationformats

ID: 44559506