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 Ca2+ binding domain within the membrane-bound region. The catalytic domain of the Ca2+-ATPase and of the NaVK+-ATPase can be interchanged by chimeric recombination without affecting the Ca2+ 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 Ca2+ binding domains appears to involve protein structural changes, most likely consisting of segmental reorientation with minimal alteration of secondary structure.

Journal Section:
Original Paper
Keywords:
Sarcoplasmic reticulum, Ca2+-ATPase, Catalytic domain, Ca2+ binding domain
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© 1994 S. Karger AG, Basel
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1994
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