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Related Experiment Videos

Octopus calmodulin. Structural comparison with bovine brain calmodulin.

K B Seamon, B W Moore

    The Journal of Biological Chemistry
    |December 25, 1980
    PubMed
    Summary
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    Octopus optic lobe protein is a calmodulin-like protein. Its structure and calcium-binding changes are similar to bovine calmodulin, despite differences in tyrosine residues.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Neuroscience

    Background:

    • Calmodulin is a key calcium-binding protein regulating cellular processes.
    • Vertebrate calmodulins have two tyrosine residues, while some invertebrates have one.

    Purpose of the Study:

    • To characterize a calmodulin-like protein from octopus optic lobe.
    • To compare its structure and calcium-binding properties with vertebrate calmodulin.

    Main Methods:

    • Amino acid composition analysis.
    • 1H Nuclear Magnetic Resonance (NMR) spectroscopy.
    • UV difference spectroscopy.

    Main Results:

    • Octopus calmodulin has one tyrosine residue, similar to Renilla reniformis calmodulin.

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  • 1H NMR and UV spectroscopy show octopus calmodulin undergoes similar calcium-induced conformational changes as bovine calmodulin.
  • The single tyrosine in octopus calmodulin is structurally homologous to tyrosine-138 in bovine calmodulin.

    • Conclusions:

    • Octopus calmodulin exhibits biochemical and structural similarities to vertebrate calmodulin.
    • Calcium-induced tertiary structure changes are conserved between octopus and bovine calmodulin, leading to similar solution conformations.