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Related Experiment Videos

A citrate-binding site in calmodulin.

T Neufeld1, M Eisenstein, K A Muszkat

  • 1Department of Molecular Microbiology and Biotechnology, George Wise Faculty of Life Sciences, Tel Aviv University, Israel.

Journal of Molecular Recognition : JMR
|March 17, 1999
PubMed
Summary
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Citrate, a common cellular molecule, alters calmodulin (CaM) structure and function by binding to it. This binding affects Ca2+ binding and the protein's overall activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Calmodulin (CaM) is a key calcium (Ca2+) sensor protein.
  • CaM regulates numerous cellular processes by activating target enzymes.
  • Ca2+ concentration influences CaM activation, suggesting modulation by chelators.

Purpose of the Study:

  • To investigate the effect of citrate, a common Ca2+ chelator, on CaM structure and function.
  • To determine if citrate binds to CaM and induces conformational changes.

Main Methods:

  • Tryptic mapping
  • Immunological recognition with monoclonal antibodies
  • CIDNP-NMR spectroscopy
  • Ligand binding assays
  • Radiolabeled citrate binding studies

Related Experiment Videos

  • X-ray crystallography analysis of citrate-binding proteins
  • Computerized molecular graphics

    • Main Results:

    • Citrate binding induces conformational modifications in CaM.
    • These structural changes affect CaM's shape and enzymatic activity.
    • Citrate binds to the C-terminal lobe of CaM, near the Ca2+-binding loop III.
    • A putative citrate-binding site (CBS) involving residues Arg106-His107 was identified.
    • Citrate binding likely alters Ca2+ binding to sites III and IV.

    Conclusions:

    • Citrate directly binds to calmodulin, causing conformational changes.
    • These changes impact Ca2+ binding and modulate CaM's functional properties.
    • Citrate acts as a modulator of CaM activity within cellular environments.