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Structural changes in the calcium pump accompanying the dissociation of calcium

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  • Chikashi Toyoshima

    (The University of Tokyo)

  • Hiromi Nomura

    (The University of Tokyo)

Abstract

In skeletal muscle, calcium ions are transported (pumped) against a concentration gradient from the cytoplasm into the sarcoplasmic reticulum, an intracellular organelle. This causes muscle cells to relax after cytosolic calcium increases during excitation. The Ca2+ ATPase that carries out this pumping is a representative P-type ion-transporting ATPase. Here we describe the structure of this ion pump at 3.1 Å resolution in a Ca2+-free (E2) state, and compare it with that determined previously for the Ca2+-bound (E1Ca2+) state. The structure of the enzyme stabilized by thapsigargin, a potent inhibitor, shows large conformation differences from that in E1Ca2+. Three cytoplasmic domains gather to form a single headpiece, and six of the ten transmembrane helices exhibit large-scale rearrangements. These rearrangements ensure the release of calcium ions into the lumen of sarcoplasmic reticulum and, on the cytoplasmic side, create a pathway for entry of new calcium ions.

Suggested Citation

  • Chikashi Toyoshima & Hiromi Nomura, 2002. "Structural changes in the calcium pump accompanying the dissociation of calcium," Nature, Nature, vol. 418(6898), pages 605-611, August.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6898:d:10.1038_nature00944
    DOI: 10.1038/nature00944
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    Cited by:

    1. 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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