The structural basis of calcium transport by the calcium pump

Claus Olesen, Martin Picard, Anne-Marie Lund Winther, Claus Gyrup, J. Preben Morth, Claus Oxvig, Jesper Vuust Møller () and Poul Nissen ()
Additional contact information
Claus Olesen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Martin Picard: University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark
Anne-Marie Lund Winther: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Claus Gyrup: University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark
J. Preben Morth: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Claus Oxvig: University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark
Jesper Vuust Møller: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Poul Nissen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,

Nature, 2007, vol. 450, issue 7172, 1036-1042

Abstract: Abstract The sarcoplasmic reticulum Ca2+-ATPase, a P-type ATPase, has a critical role in muscle function and metabolism. Here we present functional studies and three new crystal structures of the rabbit skeletal muscle Ca2+-ATPase, representing the phosphoenzyme intermediates associated with Ca2+ binding, Ca2+ translocation and dephosphorylation, that are based on complexes with a functional ATP analogue, beryllium fluoride and aluminium fluoride, respectively. The structures complete the cycle of nucleotide binding and cation transport of Ca2+-ATPase. Phosphorylation of the enzyme triggers the onset of a conformational change that leads to the opening of a luminal exit pathway defined by the transmembrane segments M1 through M6, which represent the canonical membrane domain of P-type pumps. Ca2+ release is promoted by translocation of the M4 helix, exposing Glu 309, Glu 771 and Asn 796 to the lumen. The mechanism explains how P-type ATPases are able to form the steep electrochemical gradients required for key functions in eukaryotic cells.

Date: 2007
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DOI: 10.1038/nature06418

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