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Related Experiment Videos

Crystal structure of the excisionase-DNA complex from bacteriophage lambda.

My D Sam1, Duilio Cascio, Reid C Johnson

  • 1Department of Chemistry and Biochemistry and the UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, 405 Hilgard Ave., Los Angeles, CA 90095-1570, USA.

Journal of Molecular Biology
|April 7, 2004
PubMed
Summary

Bacteriophage lambda excisionase (Xis) protein binds DNA, bending it to facilitate phage excision. Its structure reveals how Xis interacts with DNA and recruits integrase for DNA rearrangements.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Virology

Background:

  • Recombination directionality factors regulate DNA rearrangements.
  • Excisionase (Xis) protein from bacteriophage lambda is a key regulator.
  • Xis controls integrase-mediated DNA rearrangements crucial for phage life cycles.

Purpose of the Study:

  • Determine the co-crystal structure of Xis bound to its X2 DNA-binding site.
  • Elucidate the molecular interactions governing Xis-DNA recognition.
  • Provide insights into the mechanism of Xis-mediated DNA bending and integrase recruitment.

Main Methods:

  • X-ray crystallography at 1.7A resolution.
  • Co-crystallization of the Xis protein with the X2 DNA-binding site.
  • Structural analysis of protein-DNA interactions.

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Main Results:

  • The co-crystal structure reveals Xis possesses a unique winged-helix motif.
  • Xis utilizes an alpha-helix and a beta-hairpin to interact with DNA major and minor grooves, respectively.
  • Water-mediated hydrogen bonds are critical for major groove recognition, while minor groove interactions are less specific.

Conclusions:

  • The determined structure offers insights into Xis's cooperative DNA binding and integrase recruitment mechanism.
  • A potential surface for Xis-Xis interactions, essential for cooperative binding, is identified.
  • The findings suggest how Xis may significantly distort longer DNA fragments during phage excision.