Accueil > Publications > Recherche par années > Années 2000 > 2005

de Jesus, KP ; Serre, L ; Zelwer, C ; Castaing, B

Structural insights into abasic site for Fpg specific binding and catalysis : comparative high-resolution crystallographic studies of Fpg bound to various models of abasic site analogues-containing DNA

Nucleic Acids Research 33 (18) 5936-5944

par Administrateur - publié le

Abstract :

dFpg is a DNA glycosylase that recognizes and excises the mutagenic 8-oxoguanine (8-oxoG) and the potentially lethal formamidopyrimidic residues (Fapy). Fpg is also associated with an AP lyase activity which successively cleaves the abasic (AP) site at the 3’ and 5’ sides by ß delta-elimination. Here, we present the high-resolution crystal structures of the wild-type and the P1G defective mutant of Fpg from Lactococcus lactis bound to 14mer DNA duplexes containing either a tetrahydrofuran (THF) or 1,3-propanediol (Pr) AP site analogues.