1flo
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FLP RECOMBINASE-HOLLIDAY JUNCTION COMPLEX I
OverviewOverview
The crystal structure of a Flp recombinase tetramer bound to a Holliday, junction intermediate has been determined at 2.65 A resolution. Only one, of Flp's two domains, containing the active site, is structurally related, to other lambda integrase family site-specific recombinases, such as Cre., The Flp active site differs, however, in that the helix containing the, nucleophilic tyrosine is domain swapped, such that it cuts its DNA target, in trans. The Flp tetramer displays pseudo four-fold symmetry matching, that of the square planar Holliday junction substrate. This tetramer is, stabilized by additional novel trans interactions among monomers. The, structure illustrates how mechanistic unity is maintained on a chemical, level while allowing for substantial variation on the structural level, within a family of enzymes.
About this StructureAbout this Structure
1FLO is a Single protein structure of sequence from Saccharomyces cerevisiae with PHS as ligand. Structure known Active Sites: CTA, CTB, CTC, CTD and PHO. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a Flp recombinase-Holliday junction complex: assembly of an active oligomer by helix swapping., Chen Y, Narendra U, Iype LE, Cox MM, Rice PA, Mol Cell. 2000 Oct;6(4):885-97. PMID:11090626
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