1EWN

CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA

1EWN の概要

• エントリーDOI: 10.2210/pdb1ewn/pdb
• 関連するPDBエントリー: 1BNK
• 分子名称: DNA (5'-D(*GP*AP*CP*AP*TP*GP*(EDA)P*TP*TP*GP*CP*C)-3'), DNA (5'-D(P*GP*CP*AP*AP*TP*CP*AP*TP*GP*TP*CP*A)-3'), 3-METHYL-ADENINE DNA GLYCOSYLASE, ... (5 entities in total)
• 機能のキーワード: dna repair, glycosylase, aag, anpg, mpg, 3-methyladenine dna glycosylase, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 31683.75

構造登録者

Lau, A.Y.,Wyatt, M.D.,Glassner, B.J.,Samson, L.D.,Ellenberger, T. (登録日: 2000-04-26, 公開日: 2000-12-11, 最終更新日: 2024-02-07)

主引用文献

Lau, A.Y.,Wyatt, M.D.,Glassner, B.J.,Samson, L.D.,Ellenberger, T.
Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG.
Proc.Natl.Acad.Sci.USA, 97:13573-13578, 2000

PubMed Abstract: The human 3-methyladenine DNA glycosylase [alkyladenine DNA glycosylase (AAG)] catalyzes the first step of base excision repair by cleaving damaged bases from DNA. Unlike other DNA glycosylases that are specific for a particular type of damaged base, AAG excises a chemically diverse selection of substrate bases damaged by alkylation or deamination. The 2.1-A crystal structure of AAG complexed to DNA containing 1,N(6)-ethenoadenine suggests how modified bases can be distinguished from normal DNA bases in the enzyme active site. Mutational analyses of residues contacting the alkylated base in the crystal structures suggest that the shape of the damaged base, its hydrogen-bonding characteristics, and its aromaticity all contribute to the selective recognition of damage by AAG.

PubMed: 11106395
DOI: 10.1073/pnas.97.25.13573

実験手法

X-RAY DIFFRACTION (2.1 Å)