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The structure determination of rabbit phosphoglucomutase.

R K Wierenga, D G Lewis, M G Rossmann

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |June 26, 1981
    PubMed
    Summary
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    Rabbit phosphoglucomutase crystals were grown and analyzed using X-ray diffraction. Structural analysis revealed enzyme activity and stability, even after modifications to its phosphorylation and essential ions.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Crystallography

    Background:

    • Phosphoglucomutase is a key enzyme in carbohydrate metabolism.
    • Understanding its structure is crucial for elucidating its catalytic mechanism.

    Purpose of the Study:

    • To determine the three-dimensional structure of rabbit phosphoglucomutase.
    • To investigate the enzyme's properties within native crystals.

    Main Methods:

    • Crystallization of rabbit phosphoglucomutase using ammonium sulfate and polyethylene glycol.
    • X-ray diffraction data collection from native and heavy-atom derivative crystals.
    • Rotation function analysis for symmetry determination.

    Main Results:

    • Tetragonal crystals containing two enzyme molecules per asymmetric unit were obtained.

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  • A twofold rotation axis was identified relating the two molecules.
  • X-ray diffraction data allowed for partial determination of heavy-atom sites.
  • The enzyme remained active and stable in crystals, allowing phosphate and Mg2+ ion manipulation.

    • Conclusions:

    • Rabbit phosphoglucomutase can be crystallized and its structure determined by X-ray diffraction.
    • The enzyme retains activity and structural integrity in crystalline form, facilitating further structural and functional studies.