1KFV

Crystal Structure of Lactococcus lactis Formamido-pyrimidine DNA Glycosylase (alias Fpg or MutM) Non Covalently Bound to an AP Site Containing DNA.

1KFV の概要

• エントリーDOI: 10.2210/pdb1kfv/pdb
• 関連するPDBエントリー: 1EE8
• 分子名称: 5'-D(*CP*TP*CP*TP*TP*TP*(PDI)P*TP*TP*TP*CP*TP*C)-3', 5'-D(*GP*AP*GP*AP*AP*AP*CP*AP*AP*AP*GP*AP*G)-3', Formamido-pyrimidine DNA glycosylase, ... (6 entities in total)
• 機能のキーワード: dna repair enzyme, abasic site, dna, n-glycosylase, ap lyase, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Lactococcus lactis
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 78342.62

構造登録者

Serre, L.,Pereira de Jesus, K.,Boiteux, S.,Zelwer, C.,Castaing, B. (登録日: 2001-11-23, 公開日: 2002-06-14, 最終更新日: 2024-10-30)

主引用文献

Serre, L.,Pereira de Jesus, K.,Boiteux, S.,Zelwer, C.,Castaing, B.
Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA.
EMBO J., 21:2854-2865, 2002

PubMed Abstract: The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened purines, from oxidatively damaged DNA. The structure of a non-covalent complex between the Lactoccocus lactis Fpg and a 1,3-propanediol (Pr) abasic site analogue-containing DNA has been solved. Through an asymmetric interaction along the damaged strand and the intercalation of the triad (M75/R109/F111), Fpg pushes out the Pr site from the DNA double helix, recognizing the cytosine opposite the lesion and inducing a 60 degrees bend of the DNA. The specific recognition of this cytosine provides some structural basis for understanding the divergence between Fpg and its structural homologue endo nuclease VIII towards their substrate specificities. In addition, the modelling of the 8-oxoguanine residue allows us to define an enzyme pocket that may accommodate the extrahelical oxidized base.

PubMed: 12065399
DOI: 10.1093/emboj/cdf304

実験手法

X-RAY DIFFRACTION (2.55 Å)