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Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane

Nature volume 362, pages 469471 (01 April 1993) | Download Citation

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Abstract

THE ATP-driven calcium pump (Ca2+-ATPase) is an integral membrane protein (Mr 11 OK) which relaxes striated muscle by pumping calcium out of the cytoplasm into the sarcoplasmic reticulum against a large concentration gradient1. Recent efforts have attempted to relate the sequence of Ca2+-ATPase to its structure and function. In particular, site-directed mutagenesis has identified critical amino-acid residues2–6, and its predicted secondary structure, which includes ten transmembrane helices7, has gained experimental support8–10. But direct visualization of the molecule has so far been limited to the cytoplasmic domains at low resolution11, 12. We present here the three-dimensional structure of Ca2+-ATPase in the native sarcoplasmic reticulum membrane at 14 Å resolution, determined by cryo-electron microscopy and helical image analysis. The structure shows an unexpected transmembrane organization, consisting of three distinct segments, one of which is highly inclined. These features can be related to earlier predictions of secondary structure.

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Author information

Affiliations

  1. Department of Biological Sciences, Tokyo Institute of Technology, Meguro-ku, Ookayama, Tokyo 152, Japan

    • Chikashi Toyoshima
  2. Research Program, RIKEN, Wako, Saitama 351-01, Japan

    • Chikashi Toyoshima
    •  & Hiroyuki Sasabe
  3. University of Virginia Health Sciences Center, Department of Molecular Physiology and Biological Physics, Jordan Hall, Box 449, Charlottesville, Virginia 22908, USA

    • David L. Stokes
  4. To whom correspondence should be addressed.

    • David L. Stokes

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DOI

https://doi.org/10.1038/362469a0

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