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Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution

Author

Listed:
  • Peijun Zhang

    (Skirball Institute of Biomolecular Medicine, New York University Medical Center)

  • Chikashi Toyoshima

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo)

  • Koji Yonekura

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo
    Protonic Nanomachine Project, ERATO, JST)

  • N. Michael Green

    (National Institute for Medical Research)

  • David L. Stokes

    (Skirball Institute of Biomolecular Medicine, New York University Medical Center)

Abstract

The calcium pump from sarcoplasmic reticulum (Ca2+-ATPase) is typical of the large family of P-type cation pumps. These couple ATP hydrolysis with cation transport, generating cation gradients across membranes. Ca2+-ATPase specifically maintains the low cytoplasmic calcium concentration of resting muscle by pumping calcium into the sarcoplasmic reticulum; subsequent release is used to initiate contraction. No high-resolution structure of a P-type pump has yet been determined, although a 14-Å structure ofCa2+-ATPase, obtained by electron microscopy of frozen-hydrated, tubular crystals1, showed a large cytoplasmic head connected to the transmembrane domain by a narrow stalk. We have now improved the resolution to 8 Å and can discern ten transmembrane α-helices, four of which continue into the stalk. On the basis of constraints from transmembrane topology, site-directed mutagenesis and disulphide crosslinking, we have made tentative assignments for these α-helices within the amino-acid sequence. A distinct cavity leads to the putative calcium-binding site, providing a plausible path for calcium release to the lumen of the sarcoplasmic reticulum.

Suggested Citation

  • Peijun Zhang & Chikashi Toyoshima & Koji Yonekura & N. Michael Green & David L. Stokes, 1998. "Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution," Nature, Nature, vol. 392(6678), pages 835-839, April.
    • Handle: RePEc:nat:nature:v:392:y:1998:i:6678:d:10.1038_33959
    DOI: 10.1038/33959
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