4AI4

crystal structure of E38Q mutant of 3-methyladenine DNA glycosylase I from Staphylococcus aureus

4AI4 の概要

• エントリーDOI: 10.2210/pdb4ai4/pdb
• 関連するPDBエントリー: 2JG6 4AI5
• 分子名称: DNA-3-METHYLADENINE GLYCOSYLASE I, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, dna repair
• 由来する生物種: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MSSA476
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21830.03

構造登録者

Zhu, X.,Naismith, J.H. (登録日: 2012-02-08, 公開日: 2012-02-15, 最終更新日: 2023-12-20)

主引用文献

Zhu, X.,Yan, X.,Carter, L.G.,Liu, H.,Graham, S.,Coote, P.J.,Naismith, J.
A Model for 3-Methyladenine Recognition by 3-Methyladenine DNA Glycosylase I (Tag) from Staphylococcus Aureus.
Acta Crystallogr.,Sect.F, 68:610-, 2012

PubMed Abstract: The removal of chemically damaged DNA bases such as 3-methyladenine (3-MeA) is an essential process in all living organisms and is catalyzed by the enzyme 3-MeA DNA glycosylase I. A key question is how the enzyme selectively recognizes the alkylated 3-MeA over the much more abundant adenine. The crystal structures of native and Y16F-mutant 3-MeA DNA glycosylase I from Staphylococcus aureus in complex with 3-MeA are reported to 1.8 and 2.2 Å resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that charge-charge recognition is not critical for the selection of 3-MeA over adenine. It is hypothesized that the hydrogen-bonding pattern of Glu38 and Tyr16 of 3-MeA DNA glycosylase I with a particular tautomer unique to 3-MeA contributes to recognition and selection.

PubMed: 22684054
DOI: 10.1107/S1744309112016363

実験手法

X-RAY DIFFRACTION (1.73 Å)