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Related Experiment Videos

A phage repressor-operator complex at 7 A resolution.

J E Anderson, M Ptashne, S C Harrison

    Nature
    |August 15, 1985
    PubMed
    Summary
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    The crystal structure reveals how phage 434 repressor binds B-form DNA. Its helix-turn-helix motif

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Genetics

    Background:

    • Bacteriophage repressors are crucial regulators of viral gene expression.
    • Understanding DNA-protein interactions is fundamental to molecular biology.
    • The helix-turn-helix motif is a common DNA-binding structure in proteins.

    Purpose of the Study:

    • To elucidate the structural basis of phage 434 repressor binding to its operator DNA.
    • To compare the binding conformation of phage 434 repressor with related proteins like gamma repressor.

    Main Methods:

    • X-ray crystallography was used to determine the complex structure.
    • A synthetic 434 operator DNA sequence was utilized.

    Main Results:

    Related Experiment Videos

  • The crystal structure of the DNA-binding domain of phage 434 repressor complexed with synthetic 434 operator DNA was determined.
  • The protein adopts a conformation similar to gamma repressor.
  • The second alpha-helix of the helix-turn-helix motif is positioned within the major groove of B-form DNA.

    • Conclusions:

    • Phage 434 repressor binds B-form DNA via its helix-turn-helix motif.
    • Structural similarity to gamma repressor suggests conserved DNA-binding mechanisms.