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A calcium pump made visible

Lee, Anthony.G. (2002) A calcium pump made visible Current Opinion in Structural Biology, 12, (4), pp. 547-554. (doi:10.1016/S0959-440X(02)00360-3).

Record type: Article

Abstract

The first high-resolution structure of a P-type ATPase, that of the Ca2+-ATPase of skeletal muscle sarcoplasmic reticulum, was published in 2000. This structure has provided many clues to how the Ca2+-ATPase might work, but no complete answers. The Ca2+-ATPase structure reveals no clear pathway from the cytoplasmic side of the membrane to the pair of high-affinity binding sites for Ca2+ located in the transmembrane region of the ATPase and no clear pathway from these sites to the lumenal side of the membrane. The ATPase is therefore very unlike an ion channel in its construction. It is unclear from the crystal structure of the Ca2+-ATPase exactly how the protein sits within the lipid bilayer that surrounds it in the membrane. The Ca2+-ATPase is implicated in thermogenesis in some types of muscle; this could involve processes of slippage and leak modulated by interaction between the Ca2+-ATPase and sarcolipin.

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More information

Published date: 1 August 2002
Keywords: P-type ATPase, Ca2+-ATPase, ATP hydrolysis, calcium-binding sites, gating, transport, slippage, thermogenesis, sarcolipin

Identifiers

Local EPrints ID: 55957
URI: http://eprints.soton.ac.uk/id/eprint/55957
ISSN: 0959-440X
PURE UUID: c2b4e03a-4ac1-479a-8045-6a6e1a7d049c

Catalogue record

Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:31

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