Real-time studies of conformational dynamics of the repair enzyme E. coli formamidopyrimidine-DNA glycosylase and its DNA complexes during catalytic cycle

Vladimir V Koval; Nikita A Kuznetsov; Alexander A Ishchenko; Murat K Saparbaev; Olga S Fedorova

doi:10.1016/j.mrfmmm.2009.08.018

Real-time studies of conformational dynamics of the repair enzyme E. coli formamidopyrimidine-DNA glycosylase and its DNA complexes during catalytic cycle

Mutat Res. 2010 Mar 1;685(1-2):3-10. doi: 10.1016/j.mrfmmm.2009.08.018. Epub 2009 Sep 12.

Authors

Vladimir V Koval¹, Nikita A Kuznetsov, Alexander A Ishchenko, Murat K Saparbaev, Olga S Fedorova

Affiliation

¹ Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Lavrentyev Ave. 8, Novosibirsk 630090, Russia.

PMID: 19751748
DOI: 10.1016/j.mrfmmm.2009.08.018

Abstract

Fpg protein from Escherichia coli belongs to the class of DNA glycosylases/abasic site lyases excising several oxidatively damaged purines in the base excision repair pathway. In this review, we summarize the results of our studies of Fpg protein from E. coli, elucidating the intrinsic mechanism of recognition and excision of damaged bases in DNA.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Catalysis
DNA
DNA-Formamidopyrimidine Glycosylase / chemistry*
Escherichia coli Proteins / chemistry*
Kinetics
Molecular Conformation
Mutation

Substances

Escherichia coli Proteins
DNA
DNA-Formamidopyrimidine Glycosylase