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Related Experiment Videos

Crystallization and preliminary X-ray diffraction studies of beta-phosphoglucomutase from Lactococcus lactus.

Sushmita D Lahiri1, Guofeng Zhang, Peter Radstrom

  • 1Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118-2394, USA.

Acta Crystallographica. Section D, Biological Crystallography
|January 25, 2002
PubMed
Summary

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Beta-phosphoglucomutase (beta-PGM), crucial for maltose metabolism, has been crystallized. Researchers are using multiwavelength anomalous diffraction (MAD) phasing to determine its structure and understand its function within the haloacid dehalogenase superfamily.

Area of Science:

  • Enzymology
  • Structural Biology
  • Biochemistry

Background:

  • Beta-phosphoglucomutase (beta-PGM) is a 28 kDa enzyme essential for maltose metabolism.
  • It catalyzes the reversible conversion of beta-D-glucose-1-phosphate to beta-D-glucose-6-phosphate.
  • Sequence analysis reveals beta-PGM belongs to the haloacid dehalogenase (HAD) enzyme superfamily.

Purpose of the Study:

  • To determine the three-dimensional structure of beta-phosphoglucomutase.
  • To elucidate the structural basis for beta-PGM's catalytic activity within the HAD superfamily.
  • To facilitate a deeper understanding of maltose metabolism pathways.

Main Methods:

  • Crystallization of native beta-PGM using the hanging-drop method.
  • Growth of selenomethionine (SeMet)-containing beta-PGM crystals for phasing.

Related Experiment Videos

  • Collection of a three-wavelength data set to 2.3 Å using SeMet-substituted crystals.
  • Application of multiwavelength anomalous diffraction (MAD) phasing for structure solution.

    • Main Results:

    • Diffraction-quality crystals of native beta-PGM were obtained in space group P2(1)2(1)2(1) with specific unit-cell parameters.
    • SeMet-containing crystals, crucial for MAD phasing, were successfully grown via microseeding.
    • High-resolution diffraction data (2.3 Å) were collected from SeMet-substituted crystals.

    Conclusions:

    • The structural determination of beta-PGM is underway using MAD phasing.
    • Understanding beta-PGM's structure will provide insights into the catalytic mechanisms of the HAD superfamily.
    • This research contributes to the biochemical understanding of carbohydrate metabolism.