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. 1990 Sep;58(3):687–693. doi: 10.1016/S0006-3495(90)82411-5

Large-scale structural changes in the sarcoplasmic reticulum ATPase appear essential for calcium transport.

J K Blasie 1, D Pascolini 1, F Asturias 1, L G Herbette 1, D Pierce 1, A Scarpa 1
PMCID: PMC1281009  PMID: 2145042

Abstract

Model refinement calculations utilizing the results from time-resolved x-ray diffraction studies indicate that specific, large-scale changes (i.e., structural changes over a large length scale or long range) occur throughout the cylindrically averaged profile structure of the sarcoplasmic reticulum ATPase upon its phosphorylation during calcium active transport. Several physical-chemical factors, all of which slow the kinetics of phosphoenzyme formation, induce specific, large-scale changes throughout the profile structure of the unphosphorylated enzyme that in general are opposite to those observed upon phosphorylation. These results suggest that such large-scale structural changes in the ATPase occurring upon its phosphorylation are required for its calcium transport function.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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