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Nature Structural Biology  9, 643 - 645 (2002)
doi:10.1038/nsb0902-643

A P-type ion pump at work

C. Roy D. Lancaster

C. Roy D. Lancaster is in the Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Heinrich-Hoffmann-Strasse 7, D-60528 Frankfurt am Main, Germany. Roy.Lancaster@mpibp-frankfurt.mpg.de http://www.mpibp-frankfurt.mpg.de/lancaster

A second three-dimensional crystal structure of the Ca2+-ATPase from the sarcoplasmic reticulum of rabbit muscle has been determined, this time in a Ca2+-free state. Its comparison with the previously determined Ca2+-bound state reveals details of structural changes at an atomic level in the catalytic cycle of a P-type ATP-dependent cation pump.

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REFERENCE
ATPases: Ion-motive
Nature Encyclopaedia of Life Sciences

REVIEWS
Biology, structure and mechanism of P-type ATPases
Nature Reviews Molecular Cell Biology Review (01 Apr 2004)
 See all 2 matches for Reviews

NEWS AND VIEWS
Structural biology: Calcium callisthenics
Nature News and Views (08 Aug 2002)
Structural biology: Pumping ions
Nature News and Views (08 Jun 2000)
 See all 3 matches for News And Views

RESEARCH
Structural changes in the calcium pump accompanying the dissociation of calcium
Nature Article (08 Aug 2002)
Domain movements of plasma membrane H+-ATPase: 3D structures of two states by electron cryo-microscopy
The EMBO Journal Article (15 Jul 2002)
 See all 4 matches for Research

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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