Functional flexibility of Bacillus stearothermophilus formamidopyrimidine DNA-glycosylase

P Amara, L Serre - DNA repair, 2006 - Elsevier
The formamidopyrimidine-DNA glycosylase (Fpg) recognizes and eliminates efficiently 8-
oxoguanine, an abundant mutagenic DNA lesion. The X-ray structure of the inactive E3Q …

Insights into the DNA repair process by the formamidopyrimidine‐DNA glycosylase investigated by molecular dynamics

P Amara, L Serre, B Castaing, A Thomas - Protein science, 2004 - Wiley Online Library
Formamidopyrimidine‐DNA glycosylase (Fpg) identifies and removes 8‐oxoguanine from
DNA. All of the X‐ray structures of Fpg complexed to an abasic site containing DNA exhibit a …

Molecular dynamics simulation of the opposite-base preference and interactions in the active site of formamidopyrimidine-DNA glycosylase

AV Popov, AV Endutkin, YN Vorobjev… - BMC Structural …, 2018 - Springer
Abstract Background Formamidopyrimidine-DNA glycosylase (Fpg) removes abundant pre-
mutagenic 8-oxoguanine (oxoG) bases from DNA through nucleophilic attack of its N …

Substrate discrimination by formamidopyrimidine-DNA glycosylase: a mutational analysis

EI Zaika, RA Perlow, E Matz, S Broyde, R Gilboa… - Journal of Biological …, 2004 - ASBMB
Formamidopyrimidine-DNA glycosylase (Fpg) is a primary participant in the repair of 8-
oxoguanine, an abundant oxidative DNA lesion. Although the structure of Fpg has been …

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

K Song, V Hornak, C de Los Santos, AP Grollman… - Biochemistry, 2006 - ACS Publications
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 …

Substrate discrimination by formamidopyrimidine-DNA glycosylase: distinguishing interactions within the active site

RA Perlow-Poehnelt, DO Zharkov, AP Grollman… - Biochemistry, 2004 - ACS Publications
Reactive oxygen species are byproducts of normal aerobic respiration and ionizing
radiation, and they readily react with DNA to form a number of base lesions, including the …

Structural basis for the recognition of the FapydG lesion (2, 6-diamino-4-hydroxy-5-formamidopyrimidine) by formamidopyrimidine-DNA glycosylase

F Coste, M Ober, T Carell, S Boiteux, C Zelwer… - Journal of biological …, 2004 - ASBMB
Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidized
purines such as 7, 8-dihydro-8-oxoguanine (8-oxoG) and 2, 6-diamino-4-hydroxy-5 …

Energetics of lesion recognition by a DNA repair protein: Thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA …

CASA Minetti, DP Remeta, DO Zharkov… - Journal of molecular …, 2003 - Elsevier
As part of an overall effort to map the energetic landscape of the base excision repair
pathway, we report the first thermodynamic characterization of repair enzyme binding to …

Critical sites of DNA backbone integrity for damaged base removal by formamidopyrimidine–DNA glycosylase

AV Endutkin, DO Zharkov - Biochemistry, 2019 - ACS Publications
DNA glycosylases, the enzymes that initiate base excision DNA repair, recognize damaged
bases through a series of precisely orchestrated movements. Most glycosylases sharply kink …

Molecular simulations reveal a common binding mode for glycosylase binding of oxidatively damaged DNA lesions

K Song, C Kelso, C de los Santos… - Journal of the …, 2007 - ACS Publications
Cellular DNA is constantly exposed to oxidative stress from both exogenous and
endogenous sources, creating lesions that lead to aging related diseases, including cancer …