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• W2028865718 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." @default.
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• W2028865718 date "2012-05-22" @default.
• W2028865718 modified "2023-09-30" @default.
• W2028865718 title "A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from<i>Staphylococcus aureus</i>" @default.
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• W2028865718 doi "https://doi.org/10.1107/s1744309112016363" @default.
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