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The C-terminal lysine of Ogg2 DNA glycosylases is a major molecular determinant for guanine/8-oxoguanine distinction

机译：OGG2 DNA糖基酶的C末端赖氨酸是鸟嘌呤/ 8-氧通的主要分子决定因素

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摘要

7,8-dihydro-8-oxoguanine (8-oxoG) is a major oxidative lesion found in DNA. The 8-oxoguanine DNA glycosylases (Ogg) responsible for the removal of 8-oxoG are divided into three families: Ogg1, Ogg2 and AGOG. Since Ogg2 members are devoid of the recognition loop used by Ogg1 to discriminate between 8-oxoG and guanine it was unclear until recently how Ogg2 enzymes recognize the oxidized base. We present here the first crystallographic structure of an Ogg2 member, Methanocaldococcus janischii Ogg, in complex with a DNA duplex containing the 8-oxoG lesion. This structure highlights the critical role of the C-terminal lysine, strictly conserved in Ogg2, in the recognition of 8-oxoG. The structure also reveals that, similarly to Ogg1 glycosylases, Ogg2 undergoes a conformational change upon DNA binding. Furthermore, this work provides a structural rationale for the lack of opposite base specificity in this family of enzymes.

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