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Related Experiment Videos

Tertiary structure and energy coupling in Ca2(+)-pump system.

A E Shamoo1, T Lockwich, C J Cao

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

Molecular and Cellular Biochemistry
|December 20, 1990
PubMed
Summary

Europium luminescence reveals two high-affinity calcium binding sites on sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase. Enzyme structure and function are linked to dimerization for calcium uptake and hydrolysis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase is crucial for muscle contraction by regulating calcium ion concentration.
  • Understanding the calcium binding sites and their coordination is key to elucidating the enzyme's mechanism.

Purpose of the Study:

  • To investigate the number and coordination of calcium binding sites in (Ca2+ + Mg2+)-ATPase using europium luminescence.
  • To explore the role of enzyme structure, including dimerization and specific cleavage sites, in calcium binding, occlusion, and ATPase activity.

Main Methods:

  • Europium luminescence spectroscopy to probe calcium binding sites and water coordination.
  • Limited tryptic digestion at specific sites (T2, Arg 198) to assess functional consequences.

Related Experiment Videos

  • Measurement of calcium occlusion and ATPase hydrolytic activity under varying conditions (presence/absence of ATP).

    • Main Results:

    • Identified two high-affinity calcium binding sites with specific water coordination numbers (3 and 0.5).
    • ATP binding leads to further calcium occlusion (2 and 0 water molecules).
    • Tryptic digestion at T2 uncouples calcium transport from ATPase activity but preserves occlusion; further digestion affects occlusion and activity differently depending on ATP presence.

    Conclusions:

    • The dimeric form of (Ca2+ + Mg2+)-ATPase is essential for calcium occlusion and uptake.
    • Individual monomers retain ATPase hydrolytic activity, suggesting a functional specialization within the dimer.
    • Structural integrity and specific cleavage sites significantly impact the enzyme's ability to transport and hydrolyze ATP.