Comparing crystal structures of Ca2+-ATPase in the presence of different lipids

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

  • Nikolaj D Drachmann, Centre for Membrane Pumps in Cells and Disease - PUMPkin, Danish National Research Foundation, Aarhus, Denmark; Department of Molecular Biology and Genetics, Aarhus University, Denmark., Danmark
  • Claus Olesen
  • Jesper V Møller
  • Zheng Guo
  • Maike Bublitz, Danmark
  • Poul Nissen

The activity of the sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) depends strongly on the lipid composition of the surrounding membrane. Yet, structural information on SERCA-lipid interaction is still relatively scarce, and the influence of different lipids on the enzyme is not well understood. We have analyzed SERCA crystal structures in the presence of four different phosphatidylcholine lipids of different lengths and double-bond compositions, and we find three different binding sites for lipid head groups, which are apparently independent of the acyl moiety of the lipids used. By comparison with other available SERCA structures with bound lipids, we find a total of five recurring sites, two of which are specific to certain conformational states of the enzyme, two others are state-independent, and one is a crucial site for crystal formation. Three of the binding sites overlap with or are in close vicinity to known binding sites for various SERCA-specific inhibitors and regulators, e.g. thapsigargin, sarcolipin/phospholamban and cyclopiazonic acid. Whereas the transient sites are amenable to a transient, regulatory influence of lipid molecules, the state-independent sites probably provide a flexible anchoring of the protein in the fluid bilayer.

OriginalsprogEngelsk
TidsskriftF E B S Journal
Vol/bind281
Nummer18
Sider (fra-til)4249-4262
Antal sider14
ISSN1742-464X
DOI
StatusUdgivet - sep. 2014

Se relationer på Aarhus Universitet Citationsformater

ID: 83544456