Crystal structure of the calcium pump with a bound ATP analogue

Chikashi Toyoshima () and Tatsuaki Mizutani
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Chikashi Toyoshima: The University of Tokyo
Tatsuaki Mizutani: The University of Tokyo

Nature, 2004, vol. 430, issue 6999, 529-535

Abstract: 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.

Date: 2004
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DOI: 10.1038/nature02680

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