2XZU

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE WILD-TYPE LACTOCOCCUS LACTIS FPG (MUTM) AND AN OXIDIZED PYRIMIDINE CONTAINING DNA AT 310K

2XZU の概要

• エントリーDOI: 10.2210/pdb2xzu/pdb
• 関連するPDBエントリー: 1KFV 1NNJ 1PJI 1PJJ 1PM5 1TDZ 1XC8 2XZF
• 分子名称: FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE, 5'-D(*CP*TP*CP*TP*TP*TP*VETP*TP*TP*TP*CP*TP*CP*G)-3', 5'-D(GP*CP*GP*AP*GP*AP*AP*AP*CP*AP*AP*AP*G*A)-3', ... (6 entities in total)
• 機能のキーワード: hydrolase-dna complex, lyase, hydrolase/dna
• 由来する生物種: LACTOCOCCUS LACTIS; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 39810.33

構造登録者

Lebihan, Y.V.,Izquierdo, M.A.,Coste, F.,Culard, F.,Gehrke, T.H.,Essalhi, K.,Aller, P.,Carrel, T.,Castaing, B. (登録日: 2010-11-29, 公開日: 2011-10-05, 最終更新日: 2024-10-16)

主引用文献

Le Bihan, Y.V.,Izquierdo, M.A.,Coste, F.,Aller, P.,Culard, F.,Gehrke, T.H.,Essalhi, K.,Carrel, T.,Castaing, B.
5-Hydroxy-5-Methylhydantoin DNA Lesion, a Molecular Trap for DNA Glycosylases
Nucleic Acids Res., 39:6277-, 2011

PubMed Abstract: DNA base-damage recognition in the base excision repair (BER) is a process operating on a wide variety of alkylated, oxidized and degraded bases. DNA glycosylases are the key enzymes which initiate the BER pathway by recognizing and excising the base damages guiding the damaged DNA through repair synthesis. We report here biochemical and structural evidence for the irreversible entrapment of DNA glycosylases by 5-hydroxy-5-methylhydantoin, an oxidized thymine lesion. The first crystal structure of a suicide complex between DNA glycosylase and unrepaired DNA has been solved. In this structure, the formamidopyrimidine-(Fapy) DNA glycosylase from Lactococcus lactis (LlFpg/LlMutM) is covalently bound to the hydantoin carbanucleoside-containing DNA. Coupling a structural approach by solving also the crystal structure of the non-covalent complex with site directed mutagenesis, this atypical suicide reaction mechanism was elucidated. It results from the nucleophilic attack of the catalytic N-terminal proline of LlFpg on the C5-carbon of the base moiety of the hydantoin lesion. The biological significance of this finding is discussed.

PubMed: 21486746
DOI: 10.1093/NAR/GKR215

実験手法

X-RAY DIFFRACTION (1.82 Å)