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Ca2+ binding and translocation by the sarcoplasmic reticulum ATPase: functional and structural considerations

G Inesi1, L Chen, C Sumbilla

  • 1Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.

Bioscience Reports
|October 1, 1995
PubMed
Summary

The Ca(2+) ATPase in sarcoplasmic reticulum (SR) has a globular head and membrane-bound region. Phosphorylation destabilizes helices, enabling calcium transport against gradients.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Membrane Protein Function

Background:

  • The sarcoplasmic reticulum (SR) Ca(2+) ATPase is crucial for muscle contraction.
  • Understanding its mechanism is key to cellular calcium homeostasis.

Purpose of the Study:

  • To elucidate the structural and functional mechanisms of the SR Ca(2+) ATPase.
  • To investigate the relationship between enzyme phosphorylation and calcium binding/transport.

Main Methods:

  • Utilized three experimental systems: SR vesicles, reconstituted proteoliposomes, and recombinant proteins.
  • Investigated enzyme structure, including extramembranous and membrane-bound regions.
  • Analyzed cooperative calcium binding and the effects of ATP phosphorylation.

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Main Results:

  • Identified an extramembranous globular head connected to a membrane-bound region via a stalk.
  • Demonstrated sequential cooperative binding of two calcium ions within a four-helix channel.
  • Showed that ATP phosphorylation destabilizes the helical cluster, altering Ca(2+) affinity and orientation.
  • Revealed a long-range linkage between phosphorylation and Ca(2+) sites mediated by a conserved peptide segment.

Conclusions:

  • The SR Ca(2+) ATPase functions through a mechanism involving structural changes induced by phosphorylation.
  • This mechanism facilitates vectorial calcium dissociation against a concentration gradient.
  • Conserved peptide segments are critical for the enzyme's function and sensitive to mutations.