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Metal ion binding to tetrameric lima bean lectin.

M S Nissen, J A Magnuson

    The Journal of Biological Chemistry
    |February 25, 1986
    PubMed
    Summary

    Lima bean lectin binds manganese (Mn2+) and calcium (Ca2+) ions. Calcium ions reduce manganese binding and induce conformational changes in the lectin structure.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Biophysics

    Background:

    • Lectins are proteins that bind carbohydrates.
    • Lima bean lectin is a tetrameric protein with known metal-binding properties.
    • Understanding metal ion interactions is crucial for elucidating lectin function.

    Purpose of the Study:

    • To investigate the binding stoichiometry and affinity of Mn2+ and Ca2+ to lima bean lectin.
    • To characterize the conformational changes induced by metal ion binding.
    • To explore the role of specific amino acid residues in metal ion coordination.

    Main Methods:

    • Equilibrium dialysis was used to quantify metal ion binding.
    • Water proton relaxation rate enhancements monitored Mn2+ association.
    • Electron spin resonance (ESR) spectroscopy analyzed Mn2+ binding and conformational changes.
    • pH dependence studies investigated the involvement of histidine residues.

    Main Results:

    • Demetalized lectin binds 1 Mn2+ or 2 Ca2+ per monomer.
    • Pre-saturation with Ca2+ reduced Mn2+ binding to 1 per dimer.
    • Mn2+ binding induced a conformational change with an activation energy of 16 kcal/mol.
    • ESR and dialysis data indicated Ca2+ dissociates half the bound Mn2+.
    • pH dependence suggested histidine involvement in metal binding.

    Conclusions:

    • Lima bean lectin exhibits distinct binding preferences for Mn2+ and Ca2+.
    • Ca2+ binding influences Mn2+ association and induces significant conformational alterations.
    • A histidine residue likely plays a role in the metal-binding site.
    • These findings provide insights into the structural dynamics and ion-binding mechanisms of lectins.

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