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Related Experiment Videos

Structural plasticity of the Flp-Holliday junction complex.

Adam B Conway1, Yu Chen, Phoebe A Rice

  • 1Department of Biochemistry and Molecular Biology, University of Chicago, 920 E 58th Street CLSC 221, Chicago, IL 60637, USA.

Journal of Molecular Biology
|February 1, 2003
PubMed
Summary

Flp recombinase activity is regulated by protein interactions, assembling active sites in trans. A new DNA-bound Flpe structure reveals an invading 5'-OH, supporting a steric occlusion model for its unique half-of-the-sites activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Flp recombinase, a tyrosine-based site-specific recombinase, displays regulated catalytic activity via protein-protein contacts.
  • It exhibits unique half-of-the-sites activity, where active sites are assembled in trans within a tetrameric complex.
  • Isomerization of interacting protein pairs is crucial for completing the catalytic reaction.

Purpose of the Study:

  • To elucidate the structural basis of Flp recombinase's regulated activity.
  • To characterize the DNA-bound tetrameric structure of the more active Flpe variant.
  • To provide mechanistic insights into the enforcement of half-of-the-sites activity.

Main Methods:

  • X-ray crystallography of a DNA-bound tetramer of Flpe.

Related Experiment Videos

  • Structural comparison with previously determined Flp structures.
  • Analysis of protein-protein interfaces and conformational flexibility.

    • Main Results:

    • The structure of a DNA-bound Flpe tetramer was determined, revealing a tyrosine recombinase with an invading 5"-OH poised for attack.
    • Comparison with wild-type Flp structures identified differences in flexibility at distinct protein-protein interfaces within the tetramer.
    • The observed conformations define the flexibility range of the Flp complex.

    Conclusions:

    • The findings support a steric occlusion model for the enforcement of half-of-the-sites activity in Flp recombinase.
    • The structural data provides a deeper understanding of the catalytic mechanism and regulation of tyrosine recombinases.
    • Flp recombinase's unique trans-acting active site assembly and flexibility are key to its function.