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

Peijun Zhang, Chikashi Toyoshima, Koji Yonekura, N. Michael Green and David L. Stokes ()
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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
N. Michael Green: National Institute for Medical Research
David L. Stokes: Skirball Institute of Biomolecular Medicine, New York University Medical Center

Nature, 1998, vol. 392, issue 6678, 835-839

Abstract: 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.

Date: 1998
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DOI: 10.1038/33959

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