3FHG

Crystal structure of Sulfolobus solfataricus 8-oxoguanine DNA glycosylase (SsOgg)

3FHG の概要

• エントリーDOI: 10.2210/pdb3fhg/pdb
• 関連するPDBエントリー: 3FHF
• 分子名称: N-glycosylase/DNA lyase, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ogg, helix-hairpin-helix, glycosylase, 8-oxoguanine, 8-oxog, ssogg, dna damage, dna repair, glycosidase, hydrolase, lyase, multifunctional enzyme, nuclease
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25707.37

構造登録者

Faucher, F.,Doublie, S. (登録日: 2008-12-09, 公開日: 2009-05-19, 最終更新日: 2024-11-06)

主引用文献

Faucher, F.,Duclos, S.,Bandaru, V.,Wallace, S.S.,Doublie, S.
Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction.
Structure, 17:703-712, 2009

PubMed Abstract: Among the four DNA bases, guanine is particularly vulnerable to oxidative damage and the most common oxidative product, 7,8-dihydro-8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. Fortunately, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Ogg enzymes are divided into three separate families, namely, Ogg1, Ogg2, and archaeal GO glycosylase (AGOG). To date, structures of members of both Ogg1 and AGOG families are known but no structural information is available for members of Ogg2. Here we describe the first crystal structures of two archaeal Ogg2: Methanocaldococcus janischii Ogg and Sulfolobus solfataricus Ogg. A structural comparison with OGG1 and AGOG suggested that the C-terminal lysine of Ogg2 may play a key role in discriminating between guanine and 8-oxoG. This prediction was substantiated by measuring the glycosylase/lyase activity of a C-terminal deletion mutant of MjaOgg.

PubMed: 19446526
DOI: 10.1016/j.str.2009.03.007

実験手法

X-RAY DIFFRACTION (1.9 Å)