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Related Experiment Videos

Crystal structure of trp repressor/operator complex at atomic resolution.

Z Otwinowski1, R W Schevitz, R G Zhang

  • 1Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.

Nature
|September 22, 1988
PubMed
Summary
This summary is machine-generated.

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The trp repressor protein binds DNA operator sequences not by directly contacting bases, but indirectly by sensing DNA shape. This binding specificity arises from interactions with the DNA

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The trp repressor is a key regulator of tryptophan biosynthesis in bacteria.
  • Understanding repressor-operator interactions is crucial for gene regulation studies.

Purpose of the Study:

  • To elucidate the molecular basis of trp repressor specificity for its DNA operator sequence.
  • To determine the structural determinants of the trp repressor/operator complex.

Main Methods:

  • X-ray crystallography was used to determine the structure of the trp repressor/operator complex.
  • Analysis of hydrogen bonding and non-polar contacts within the complex.

Main Results:

  • The trp repressor/operator complex exhibits an extensive contact surface with 24 direct and 6 solvent-mediated hydrogen bonds to DNA phosphate groups.

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  • No direct hydrogen bonds or non-polar contacts to DNA bases were found that explain specificity.
  • Sequence specificity is achieved indirectly through the repressor's recognition of DNA backbone geometry.
  • Water-mediated polar contacts to bases also contribute to specificity.

    • Conclusions:

    • The trp repressor recognizes its operator sequence primarily through indirect interactions with the DNA phosphate backbone and its induced geometry.
    • Specificity is a complex interplay of direct and indirect contacts, including water-mediated interactions.