1m6x
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Flpe-Holliday Junction Complex
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1M6X is a [Protein complex] structure of sequences from [Saccharomyces cerevisiae]. Structure known Active Sites: CTA, CTB, CTC and CTD. Full crystallographic information is available from [OCA].
ReferenceReference
Structural plasticity of the Flp-Holliday junction complex., Conway AB, Chen Y, Rice PA, J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:12559911
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