Computational analysis of the mode of binding of 8-oxoguanine to formamidopyrimidine-DNA glycosylase.

ABSTRACT: 8-Oxoguanine (8OG) is the most prevalent form of oxidative DNA damage. In bacteria, 8OG is excised by formamidopyrimidine glycosylase (Fpg) as the initial step in base excision repair. To efficiently excise this lesion, Fpg must discriminate between 8OG and an excess of guanine in duplex DNA. In this study, we explore the structural basis underlying this high degree of selectivity. Two structures have been reported in which Fpg is bound to DNA, differing with respect to the position of the lesion in the active site, one structure showing 8OG bound in the syn conformation and the other in the anti conformation. Remarkably, the results of our all-atom simulations are consistent with both structures. The syn conformation observed in the crystallographic structure of Fpg obtained from Bacillus

SUBMITTER: Song K 

PROVIDER: S-EPMC8295719 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature