The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm

Anne-Marie L. Winther, Maike Bublitz, Jesper L. Karlsen, Jesper V. Møller, John B. Hansen, Poul Nissen () and Morten J. Buch-Pedersen ()
Additional contact information
Anne-Marie L. Winther: Pcovery, Thorvaldsensvej 57, DK-1871 Frederiksberg, Denmark
Maike Bublitz: Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
Jesper L. Karlsen: Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
Jesper V. Møller: Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
John B. Hansen: Pcovery, Thorvaldsensvej 57, DK-1871 Frederiksberg, Denmark
Poul Nissen: Centre for Membrane Pumps in Cells and Disease—PUMPkin, Danish National Research Foundation
Morten J. Buch-Pedersen: Pcovery, Thorvaldsensvej 57, DK-1871 Frederiksberg, Denmark

Nature, 2013, vol. 495, issue 7440, 265-269

Abstract: An X-ray crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) in the presence of sarcolipin, a SERCA regulator, is presented; the structure shows that sarcolipin traps SERCA in a previously unidentified ‘open’ state in which its high-affinity Ca2+-binding sites are unoccupied, but accessible from the cytoplasm.

Date: 2013
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DOI: 10.1038/nature11900

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