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The structural basis of calcium transport by the calcium pump

Author

Listed:
  • Claus Olesen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    Institute of Physiology and Biophysics, University of Aarhus, Ole Worms Alle, blg. 1185, DK - 8000 Aarhus C, Denmark)

  • Martin Picard

    (University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark
    Present address: Laboratoire de Cristallographie et RMN biologiques, UMR 8015 CNRS, Faculté de Pharmacie. Université Paris Descartes, 4 avenue de l'Observatoire, 75270 Paris Cedex 06, France.)

  • Anne-Marie Lund Winther

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark)

  • 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,
    University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark)

  • 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,
    Institute of Physiology and Biophysics, University of Aarhus, Ole Worms Alle, blg. 1185, DK - 8000 Aarhus C, Denmark)

  • Poul Nissen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    University of Aarhus, Gustav Wieds Vej 10C, DK - 8000 Aarhus C, Denmark)

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.

Suggested Citation

  • Claus Olesen & Martin Picard & Anne-Marie Lund Winther & Claus Gyrup & J. Preben Morth & Claus Oxvig & Jesper Vuust Møller & Poul Nissen, 2007. "The structural basis of calcium transport by the calcium pump," Nature, Nature, vol. 450(7172), pages 1036-1042, December.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06418
    DOI: 10.1038/nature06418
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    Cited by:

    1. Phong T. Nguyen & Christine Deisl & Michael Fine & Trevor S. Tippetts & Emiko Uchikawa & Xiao-chen Bai & Beth Levine, 2022. "Structural basis for gating mechanism of the human sodium-potassium pump," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Bjørn P Pedersen & Georgiana Ifrim & Poul Liboriussen & Kristian B Axelsen & Michael G Palmgren & Poul Nissen & Carsten Wiuf & Christian N S Pedersen, 2014. "Large Scale Identification and Categorization of Protein Sequences Using Structured Logistic Regression," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-11, January.
    3. Yingying Guo & Yuanyuan Zhang & Renhong Yan & Bangdong Huang & Fangfei Ye & Liushu Wu & Ximin Chi & Yi shi & Qiang Zhou, 2022. "Cryo-EM structures of recombinant human sodium-potassium pump determined in three different states," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    4. Peng Zhao & Chaoran Zhao & Dandan Chen & Caihong Yun & Huilin Li & Lin Bai, 2021. "Structure and activation mechanism of the hexameric plasma membrane H+-ATPase," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    5. Zongxin Guo & Fredrik Orädd & Viktoria Bågenholm & Christina Grønberg & Jian Feng Ma & Peter Ott & Yong Wang & Magnus Andersson & Per Amstrup Pedersen & Kaituo Wang & Pontus Gourdon, 2024. "Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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