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Related Experiment Videos

SERCA structural dynamics induced by ATP and calcium.

Benjamin Mueller1, Min Zhao, Igor V Negrashov

  • 1Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota Medical School, Jackson Hall 6-155, 312 Church Street, Minneapolis, Minnesota 55455, USA.

Biochemistry
|October 6, 2004
PubMed
Summary

This study reveals that adenosine 5'-triphosphate (ATP) significantly influences the structural dynamics of calcium-dependent ATPase (SERCA), more so than calcium (Ca) itself. These findings challenge previous hypotheses about Ca-induced structural changes in SERCA.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzyme Kinetics

Background:

  • Sarcoplasmic reticulum calcium ATPase (SERCA) is crucial for muscle contraction.
  • X-ray crystallography suggests large structural changes induced by calcium (Ca).
  • Previous studies used probes that inactivated the enzyme.

Purpose of the Study:

  • To investigate the rotational dynamics of active SERCA using time-resolved phosphorescence anisotropy (TPA).
  • To test the hypothesis that Ca induces large-scale structural changes in SERCA.
  • To differentiate the effects of Ca and adenosine 5 omino-triphosphate (ATP) on SERCA dynamics.

Main Methods:

  • Time-resolved phosphorescence anisotropy (TPA) was used to probe SERCA rotational dynamics.
  • SERCA was labeled with erythrosin 5 omino-iodoacetamide, targeting the phosphorylation domain.

Related Experiment Videos

  • Effects of Ca, ATP, and a non-hydrolyzable ATP analogue on labeled SERCA were analyzed.

    • Main Results:

    • ATP binding induced a significant tilting (≥20 degrees) of the phosphorylation domain.
    • These ATP-induced changes were independent of active ion transport.
    • Melittin abolished nucleotide-induced dynamics and increased anisotropy, suggesting aggregation-induced inhibition.

    Conclusions:

    • SERCA structural changes are more dependent on ATP than Ca, contrary to crystallographic hypotheses.
    • Aggregation-induced inhibition of SERCA involves functional coupling between global and internal protein dynamics.