1M6X

Flpe-Holliday Junction Complex

Summary for 1M6X

• Entry DOI: 10.2210/pdb1m6x/pdb
• Related: 1FLO
• Descriptor: Symmetrized FRT site, Flp recombinase, ... (5 entities in total)
• Functional Keywords: tyrosine recombinase, protein-dna complex, holliday-junction, domain-swapping, ligase, lyase-dna complex, lyase/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 10
• Total formula weight: 235247.17

Authors

Conway, A.B.,Chen, Y.,Rice, P.A. (deposition date: 2002-07-17, release date: 2003-02-04, Last modification date: 2024-10-30)

Primary citation

Conway, A.B.,Chen, Y.,Rice, P.A.
Structural Plasticity of the Flp-Holliday Junction Complex
J.Mol.Biol., 326:425-434, 2003

PubMed Abstract: The Flp recombinase, a member of the lambda integrase or tyrosine-based family of site-specific recombinases, is an interesting example of an enzyme whose catalytic activity is regulated by protein-protein contacts. It exhibits half-of-the-sites activity throughout its catalytic cycle. Flp is unique among these recombinases, in that it assembles each active site in trans through the interaction of two protein monomers within the catalytic tetramer, with isomerization of interacting pairs being essential to complete a full reaction. We report here the structure of a DNA-bound tetramer of Flpe, a variant of Flp that is more active at 37 degrees C than the wild-type recombinase. This new structure includes the first observation of a tyrosine recombinase with an invading 5'-OH poised to attack the covalent phosphotyrosine residue. Comparison with the previously determined Flp structure highlights differences in flexibility between the two types of protein-protein interfaces in the tetramer and better defines the range of conformations available to this remarkably flexible complex. These results suggest a steric occlusion model for enforcement of half-of-the-sites activity.

PubMed: 12559911
DOI: 10.1016/S0022-2836(02)01370-0

Experimental method

X-RAY DIFFRACTION (2.8 Å)