1FLO

FLP Recombinase-Holliday Junction Complex I

1FLO の概要

• エントリーDOI: 10.2210/pdb1flo/pdb
• 分子名称: SYMMETRIZED FRT DNA SITES, FLP RECOMBINASE, PHOSPHONIC ACID, ... (5 entities in total)
• 機能のキーワード: tyrosine recombinase, protein-dna complex, holliday-junction, domain-swapping, ligase, lyase-dna complex, lyase/dna
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 235101.11

構造登録者

Chen, Y.,Narendra, U.,Iype, L.E.,Cox, M.M.,Rice, P.A. (登録日: 2000-08-14, 公開日: 2000-09-04, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.65 Å)