Theme and Variation in Tyrosine Recombinases: Structure of a Flp-DNA Complex

摘要: The recently determined structure of a Flp-DNA complex confirms that its catalytic domain closely resembles other family members, although the active site itself is assembled differently. reaction mechanism as drawn distillation years work by many laboratories. In addition to complex, which focus this chapter, crystal structures four members have been determined: core domains λ (30) and HP1 (23) phage integrases, intact Escherichia coli XerD (52), bacteriophage P1 Cre. Flp has known for some time differ from relatives in one very important aspect: contrast tyrosine recombinases, including Cre (20), XerC D (5, 7), sites within complexes are composed amino acid residues two different monomers. chapter briefly describes Flp-Holliday junction biochemical implications, explores similarities differences recombinases type IB topoisomerases.