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Phosphoglycerate kinase.

C C Blake, D W Rice

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |June 26, 1981
    PubMed
    Summary
    This summary is machine-generated.

    Phosphoglycerate kinase (PGK) facilitates ATP production via phosphoryl transfer. Structural studies reveal conserved domains in horse and yeast PGK, suggesting a hinge-bending mechanism for substrate binding and catalysis.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Enzymology

    Background:

    • Phosphoglycerate kinase (PGK) is a crucial enzyme in glycolysis.
    • It catalyzes the ATP-producing reaction between 1,3-bisphosphoglycerate and ADP, requiring magnesium ions.
    • PGK is a highly conserved monomeric enzyme found across various species.

    Purpose of the Study:

    • To elucidate the molecular structure of phosphoglycerate kinase.
    • To understand the substrate binding sites and catalytic mechanism.
    • To compare the structure of PGK from different species, specifically horse muscle and yeast.

    Main Methods:

    • X-ray crystallography was used to determine the three-dimensional structure of horse muscle and yeast PGK.
    • Amino acid sequencing of the horse enzyme was performed.

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  • Substrate binding studies were conducted.
  • Solution studies provided evidence for conformational changes.

    • Main Results:

    • The molecular structures of horse and yeast PGK are highly similar.
    • The enzyme comprises two distinct domains (N-terminal and C-terminal) formed from the polypeptide chain.
    • Substrates bind to separate domains, approximately 12 Å apart.
    • A hinge-bending conformational change is proposed to facilitate substrate interaction for catalysis.
    • Crystals of a ternary complex of horse PGK were obtained.

    Conclusions:

    • The conserved two-domain structure of PGK supports a hinge-bending mechanism for catalysis.
    • This conformational change is essential for bringing substrates together.
    • Structural insights provide a basis for understanding PGK function and evolution.