Global conformational dynamics of a Y-family DNA polymerase during catalysis

ABSTRACT: Numerous kinetic, structural, and theoretical studies have established that DNA polymerases adjust their domain structures to enclose nucleotides in their active sites and then rearrange critical active site residues and substrates for catalysis, with the latter conformational change acting to kinetically limit the correct nucleotide incorporation rate. Additionally, structural studies have revealed a large conforma-tional change between the apoprotein and the DNA−protein binary state for Y-family DNA polymerases. In previous studie