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Distinct structural identities of catalytic and Ca-2+ binding domains in the sarcoplasmic reticulum ATPase



Distinct structural identities of catalytic and Ca-2+ binding domains in the sarcoplasmic reticulum ATPase



Cellular Physiology & Biochemistry 4(3-4): 135-147



Electron microscopic visualization and diffraction patterns yield a profile for the 110-kD SR ATPase, which includes a globular cytosolic region connected through a stalk to a membrane-bound region. Chemical derivatization and mutagenesis demonstrate that the catalytic domain is located within the cytosolic region and the Ca-2+ binding domain within the membrane-bound region. The catalytic domain of the Ca-2+-ATPase and of the Na+/K+-ATPase can be interchanged by chimeric recombination without affecting the Ca-2+ binding domain. Considerable detail of the ATPase folding pattern and functional structures is obtained by spectroscopic experiments and molecular modelling. The long-range functional linkage between the catalytic and Ca-2+ binding domains appears to involve protein structural changes, most likely consisting of segmental reorientation with minimal alteration of secondary structure.

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Accession: 008487968

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DOI: 10.1159/000154717


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