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Crystal structure of the sodium–potassium pump

Author

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  • 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)

  • Bjørn P. Pedersen

    (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)

  • Mads S. Toustrup-Jensen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    Institute of Physiology and Biophysics, University of Aarhus, Ole Worms Allé, Blg. 1160, DK-8000 Aarhus C, Denmark)

  • Thomas L.-M. Sørensen

    (University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
    Present address: Diamond Light Source Ltd, Diamond House, Chilton, Didcot, Oxfordshire, OX11 0DE, UK.)

  • Janne Petersen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    Institute of Physiology and Biophysics, University of Aarhus, Ole Worms Allé, Blg. 1160, DK-8000 Aarhus C, Denmark)

  • Jens Peter Andersen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    Institute of Physiology and Biophysics, University of Aarhus, Ole Worms Allé, Blg. 1160, DK-8000 Aarhus C, Denmark)

  • Bente Vilsen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
    Institute of Physiology and Biophysics, University of Aarhus, Ole Worms Allé, Blg. 1160, 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 Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 Å resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the α-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The β- and γ-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices αM7/αM10 and αM9, respectively. The γ-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the α-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential.

Suggested Citation

  • J. Preben Morth & Bjørn P. Pedersen & Mads S. Toustrup-Jensen & Thomas L.-M. Sørensen & Janne Petersen & Jens Peter Andersen & Bente Vilsen & Poul Nissen, 2007. "Crystal structure of the sodium–potassium pump," Nature, Nature, vol. 450(7172), pages 1043-1049, December.
    • Handle: RePEc:nat:nature:v:450:y:2007:i:7172:d:10.1038_nature06419
    DOI: 10.1038/nature06419
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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. 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.
    3. 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.
    4. Victoria C. Young & Hanayo Nakanishi & Dylan J. Meyer & Tomohiro Nishizawa & Atsunori Oshima & Pablo Artigas & Kazuhiro Abe, 2022. "Structure and function of H+/K+ pump mutants reveal Na+/K+ pump mechanisms," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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