1FLO

FLP Recombinase-Holliday Junction Complex I

Summary for 1FLO

• Entry DOI: 10.2210/pdb1flo/pdb
• Descriptor: SYMMETRIZED FRT DNA SITES, FLP RECOMBINASE, PHOSPHONIC ACID, ... (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)
• Total number of polymer chains: 12
• Total formula weight: 235101.11

Authors

Chen, Y.,Narendra, U.,Iype, L.E.,Cox, M.M.,Rice, P.A. (deposition date: 2000-08-14, release date: 2000-09-04, Last modification date: 2024-02-07)

Primary citation

Chen, Y.,Narendra, U.,Iype, L.E.,Cox, M.M.,Rice, P.A.
Crystal structure of a Flp recombinase-Holliday junction complex: assembly of an active oligomer by helix swapping.
Mol.Cell, 6:885-897, 2000

PubMed Abstract: 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.

PubMed: 11090626
DOI: 10.1016/S1097-2765(00)00086-1

Experimental method

X-RAY DIFFRACTION (2.65 Å)