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

Academic Article
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Overview

authors

  • Blasie, J. K.
  • Pascolini, D.
  • Asturias, Francisco
  • Herbette, L. G.
  • Pierce, D.
  • Scarpa, A.

publication date

  • September 1990

journal

  • Biophysical Journal  Journal

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.

subject areas

  • Biological Transport, Active
  • Calcium
  • Calcium-Transporting ATPases
  • Models, Biological
  • Protein Conformation
  • Sarcoplasmic Reticulum
  • Structure-Activity Relationship
  • X-Ray Diffraction
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Identity

PubMed Central ID

  • PMC1281009

International Standard Serial Number (ISSN)

  • 0006-3495

Digital Object Identifier (DOI)

  • 10.1016/S0006-3495(90)82411-5

PubMed ID

  • 2145042
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Additional Document Info

start page

  • 687

end page

  • 693

volume

  • 58

issue

  • 3

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