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Crystallizing catabolite gene activator protein with cAMP for structural analysis.

I T Weber

    Methods in Enzymology
    |January 1, 1988
    PubMed
    Summary

    The crystal structure of the catabolite activator protein (CAP) dimer bound to cyclic AMP (cAMP) reveals its gene regulatory function. This structure illuminates how CAP interacts with DNA and models cAMP-binding domains in other proteins.

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    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Biochemistry

    Background:

    • The catabolite activator protein (CAP) is a crucial gene regulatory protein.
    • Understanding CAP's structure is key to deciphering its function in gene expression.
    • Cyclic AMP (cAMP) is a vital second messenger involved in cellular signaling.

    Purpose of the Study:

    • To elucidate the three-dimensional structure of the CAP dimer in complex with cAMP.
    • To gain insights into the molecular mechanisms of CAP-mediated gene regulation.
    • To compare CAP's structural features with other related gene regulatory proteins.

    Main Methods:

    • X-ray crystallography was employed to determine the high-resolution crystal structure.
    • Biochemical assays were used to confirm protein-DNA and protein-cAMP interactions.

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  • Comparative structural analysis was performed against known gene regulatory proteins.

    • Main Results:

    • The crystal structure revealed a dimeric CAP molecule with distinct amino-terminal and carboxy-terminal domains connected by a hinge region.
    • The carboxy-terminal domains exhibit significant sequence and structural homology with other bacterial and viral gene regulatory proteins, indicating conserved DNA-binding mechanisms.
    • The amino-terminal domain forms the cAMP-binding pocket and serves as a model for cAMP-binding domains in eukaryotic systems, such as mammalian cAMP-dependent protein kinase.

    Conclusions:

    • The determined structure provides a detailed molecular basis for CAP's function as a transcriptional activator.
    • CAP's modular domain structure facilitates its interaction with both DNA and cAMP.
    • The structural similarities highlight evolutionary conservation in gene regulation across different organisms.