Article
Restoration of catalytic functions in Cre recombinase mutants by electrostatic compensation between active site and DNA substrate.
Nucleic acids research - 1 Oct 2010
Kachroo Aashiq H, Ma Chien-Hui, Rowley Paul A, Maciaszek Anna D, Guga Piotr, Jayaram Makkuni
Abstract excerpt
Two conserved catalytic arginines, Arg-173 and Arg-292, of the tyrosine site-specific recombinase Cre are essential for the transesterification steps of strand cleavage and joining in native DNA substrates containing scissile phosphate groups. The active site tyrosine (Tyr-324) provides the nucleophile for the cleavage reaction, and forms a covalent 3'-phosphotyrosyl intermediate. The 5'-hydroxyl group formed...
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