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Crystal structure of lambda-Cro bound to a consensus operator at 3.0 A resolution

R A Albright1, B W Matthews

  • 1Institute of Molecular Biology Howard Hughes Medical Institute and Department of Physics, University of Oregon, Eugene, OR, 97403-1229, USA.

Journal of Molecular Biology
|July 7, 1998
PubMed
Summary

The bacteriophage lambda Cro protein

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Area of Science:

  • Structural Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Bacteriophage lambda Cro protein regulates gene expression.
  • Understanding Cro-DNA interactions is crucial for molecular biology.
  • Previous studies indicated significant conformational changes upon binding.

Purpose of the Study:

  • To determine the high-resolution crystal structure of the Cro protein-DNA complex.
  • To elucidate the detailed molecular interactions between Cro and its operator DNA.
  • To understand the mechanism of DNA operator recognition and discrimination.

Main Methods:

  • X-ray crystallography at 3.0 A resolution.
  • Analysis of protein-DNA complex structure.
  • Comparison with free protein structure and biochemical data.

Main Results:

  • Detailed interactions between Cro side-chains and operator base-pairs revealed.
  • Significant conformational changes observed: 53-degree subunit rotation in Cro and 40-degree DNA bending.
  • Operator recognition primarily via hydrogen bonding and van der Waals contacts in the major groove.
  • Discrimination between similar operators (OR3 vs. OR1) involves a combination of direct and indirect effects, with one van der Waals contact being key.

Conclusions:

  • The high-resolution structure confirms and details previous low-resolution findings.
  • Cro-DNA binding involves substantial protein and DNA structural rearrangements.
  • Operator recognition is mediated by direct molecular contacts, with specific van der Waals interactions playing a critical role in sequence discrimination.

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