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Crystal structure of the calcium pump with a bound ATP analogue

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  • Chikashi Toyoshima

    (The University of Tokyo)

  • Tatsuaki Mizutani

    (The University of Tokyo)

Abstract

P-type ATPases are ATP-powered ion pumps that establish ion concentration gradients across cell and organelle membranes. Here, we describe the crystal structure of the Ca2+ pump of skeletal muscle sarcoplasmic reticulum, a representative member of the P-type ATPase superfamily, with an ATP analogue, a Mg2+ and two Ca2+ ions in the respective binding sites. In this state, the ATP analogue reorganizes the three cytoplasmic domains (A, N and P), which are widely separated without nucleotide, by directly bridging the N and P domains. The structure of the P-domain itself is altered by the binding of the ATP analogue and Mg2+. As a result, the A-domain is tilted so that one of the transmembrane helices moves to lock the cytoplasmic gate of the transmembrane Ca2+-binding sites. This appears to be the mechanism for occluding the bound Ca2+ ions, before releasing them into the lumen of the sarcoplasmic reticulum.

Suggested Citation

  • Chikashi Toyoshima & Tatsuaki Mizutani, 2004. "Crystal structure of the calcium pump with a bound ATP analogue," Nature, Nature, vol. 430(6999), pages 529-535, July.
    • Handle: RePEc:nat:nature:v:430:y:2004:i:6999:d:10.1038_nature02680
    DOI: 10.1038/nature02680
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    Cited by:

    1. 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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