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Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

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  • Chikashi Toyoshima

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku
    The Harima Institute, The Institute of Physical and Chemical Research, Sayo-gun)

  • Masayoshi Nakasako

    (Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku
    The Harima Institute, The Institute of Physical and Chemical Research, Sayo-gun
    PRESTO, Japan Science and Technology Corporation)

  • Hiromi Nomura

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

  • Haruo Ogawa

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

Abstract

Calcium ATPase is a member of the P-type ATPases that transport ions across the membrane against a concentration gradient. Here we have solved the crystal structure of the calcium ATPase of skeletal muscle sarcoplasmic reticulum (SERCA1a) at 2.6 Å resolution with two calcium ions bound in the transmembrane domain, which comprises ten α-helices. The two calcium ions are located side by side and are surrounded by four transmembrane helices, two of which are unwound for efficient coordination geometry. The cytoplasmic region consists of three well separated domains, with the phosphorylation site in the central catalytic domain and the adenosine-binding site on another domain. The phosphorylation domain has the same fold as haloacid dehalogenase. Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport.

Suggested Citation

  • Chikashi Toyoshima & Masayoshi Nakasako & Hiromi Nomura & Haruo Ogawa, 2000. "Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution," Nature, Nature, vol. 405(6787), pages 647-655, June.
    • Handle: RePEc:nat:nature:v:405:y:2000:i:6787:d:10.1038_35015017
    DOI: 10.1038/35015017
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    Cited by:

    1. 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.

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