Crystal structure of the bacteriophage P2 integrase catalytic domain

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Abstract

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.

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Skaar, K., Claesson, M., Odegrip, R., Högbom, M., Haggård-Ljungquist, E., & Stenmark, P. (2015). Crystal structure of the bacteriophage P2 integrase catalytic domain. FEBS Letters, 589(23), 3556–3563. https://doi.org/10.1016/j.febslet.2015.09.026

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