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Related Experiment Videos

Metal ion binding in triclinic lysozyme.

K Kurachi, L C Sieker, L H Jensen

    The Journal of Biological Chemistry
    |October 10, 1975
    PubMed
    Summary
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    Metal ions manganese (Mn2+), cobalt (Co2+), and gadolinium (Gd3+) binding sites were identified in triclinic lysozyme. These ions bind near the Glu-35 residue, with Gd3+ also showing a secondary site near Asp-52.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Protein-ligand interactions

    Background:

    • Lysozyme is a crucial enzyme in biological systems.
    • Understanding metal ion interactions with proteins is vital for comprehending their function and stability.
    • Triclinic lysozyme serves as a model system for studying protein-metal interactions.

    Purpose of the Study:

    • To determine the precise binding sites and occupancies of Mn2+, Co2+, and Gd3+ in triclinic lysozyme.
    • To investigate the binding site of Mn2+ in the di(N-acetylglucosamine)-lysozyme complex.
    • To elucidate the structural basis of metal ion coordination in lysozyme.

    Main Methods:

    • X-ray crystallography was employed to determine the three-dimensional structures.
    • High-resolution structural analysis was performed at specific pH conditions (4.5-4.6).

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  • Coordination environments and ion occupancies were quantified.

    • Main Results:

    • Mn2+ and Co2+ bind to a primary site near Glu-35 (2.5 A from an oxygen atom).
    • Gd3+ binds to two sites: a primary site near Glu-35 and a secondary site near Asp-52 (3.1 A from an oxygen atom).
    • Observed ion occupancies were generally low, indicating specific but limited binding.

    Conclusions:

    • The study precisely mapped metal ion binding sites in triclinic lysozyme.
    • The findings highlight the specific coordination preferences of Mn2+, Co2+, and Gd3+ with lysozyme residues.
    • Mn2+ binding in the di(N-acetylglucosamine)-lysozyme complex is similar to native lysozyme but with reduced occupancy.