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Crystal structure of the bacteriophage P2 integrase catalytic domain
Author(s) -
Skaar Karin,
Claesson Magnus,
Odegrip Richard,
Högbom Martin,
Haggård-Ljungquist Elisabeth,
Stenmark Pål
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.09.026
Subject(s) - integrase , integrases , bacteriophage , dna , temperateness , genome , site specific recombination , biology , cre lox recombination , genetics , chemistry , gene , recombination , escherichia coli , recombinase , transgene , genetically modified mouse
Bacteriophage P2 is a temperate phage capable of integrating its DNA into the host genome by site‐specific recombination upon lysogenization. Integration and excision of the phage genome requires P2 integrase, which performs recognition, cleavage and joining of DNA during these processes. This work presents the high‐resolution crystal structure of the catalytic domain of P2 integrase, and analysis of the structure–function relationship of several previously identified non‐functional P2 integrase mutants. The DNA binding area is characterized by a large positively charged patch, harboring key residues. The structure reveals potential for large dimer flexibility, likely essential for rearrangement of DNA strands upon integration and excision of the phage DNA.