Conformational dynamics of a Y-family DNA polymerase during substrate binding and catalysis as revealed by interdomain Forster resonance energy transfer.

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 conformational change between the apoprotein and the DNA-protein binary state for Y-family DNA polymerases. In previous studies [Xu, C., Maxwell, B. A., Brown, J. A., Zhang, L., and Suo, Z. (2009) PLoS Biol. 7, e1000225], a real-time Förster resonance energy transfer (FRET) method was developed to monitor the global conformational transitions of DNA polymerase IV from Sulfolobus solfata

SUBMITTER: Maxwell BA 

PROVIDER: S-EPMC3985488 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature