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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-A structure of Ca2+-ATPase, obtained by electron microscopy of frozen-hydrated, tubular crystals, showed a large cytoplasmic head connected to the transmembrane domain by a narrow stalk. We have now improved the resolution to 8A and can discern ten transmembrane alpha-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 alpha-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.

Original publication

DOI

10.1038/33959

Type

Journal article

Journal

Nature

Publication Date

23/04/1998

Volume

392

Pages

835 - 839

Keywords

Amino Acid Sequence, Animals, Calcium-Transporting ATPases, Crystallography, Image Processing, Computer-Assisted, Models, Molecular, Molecular Sequence Data, Protein Conformation, Rabbits, Rats, Saccharomyces cerevisiae, Sarcoplasmic Reticulum, Sheep