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Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state

Author

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  • Ryuta Kanai

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan)

  • Haruo Ogawa

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan)

  • Bente Vilsen

    (Aarhus University, 8000 Aarhus C, Denmark)

  • Flemming Cornelius

    (Aarhus University, 8000 Aarhus C, Denmark)

  • Chikashi Toyoshima

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan)

Abstract

Na+,K+-ATPase pumps three Na+ ions out of cells in exchange for two K+ taken up from the extracellular medium per ATP molecule hydrolysed, thereby establishing Na+ and K+ gradients across the membrane in all animal cells. These ion gradients are used in many fundamental processes, notably excitation of nerve cells. Here we describe 2.8 Å-resolution crystal structures of this ATPase from pig kidney with bound Na+, ADP and aluminium fluoride, a stable phosphate analogue, with and without oligomycin that promotes Na+ occlusion. These crystal structures represent a transition state preceding the phosphorylated intermediate (E1P) in which three Na+ ions are occluded. Details of the Na+-binding sites show how this ATPase functions as a Na+-specific pump, rejecting K+ and Ca2+, even though its affinity for Na+ is low (millimolar dissociation constant). A mechanism for sequential, cooperative Na+ binding can now be formulated in atomic detail.

Suggested Citation

  • Ryuta Kanai & Haruo Ogawa & Bente Vilsen & Flemming Cornelius & Chikashi Toyoshima, 2013. "Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state," Nature, Nature, vol. 502(7470), pages 201-206, October.
    • Handle: RePEc:nat:nature:v:502:y:2013:i:7470:d:10.1038_nature12578
    DOI: 10.1038/nature12578
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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.

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