A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus.

Xiaofeng Zhu, Xuan Yan, Lester G Carter, Huanting Liu, Shirley Graham, Peter J Coote, James Naismith
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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.

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金黄色葡萄球菌 3-甲基腺嘌呤 DNA 糖基化酶 I (TAG) 识别 3-甲基腺嘌呤的模型。
清除化学损伤的 DNA 碱基(如 3-甲基腺嘌呤 (3-MeA))是所有生物体内的一个基本过程,由 3-MeA DNA 糖基化酶 I 催化。一个关键问题是该酶如何选择性地识别烷基化的 3-MeA 而不是含量更高的腺嘌呤。据报道,来自金黄色葡萄球菌的原生和 Y16F 突变的 3-MeA DNA 糖基化酶 I 与 3-MeA 复合物的晶体结构分辨率分别为 1.8 和 2.2 Å。等温滴定量热法显示,3-MeA 的质子化会降低其结合亲和力,这证实了之前的荧光研究,即电荷识别对于选择 3-MeA 而不是腺嘌呤并不重要。据推测,3-MeA DNA 糖基化酶 I 的 Glu38 和 Tyr16 与 3-MeA 独有的特定同系物的氢键模式有助于识别和选择。
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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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