Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA
Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA
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DOI：
10.1038/emboj.2011.313
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发表时间：
2011-11-02
期刊：
影响因子：
11.4
通讯作者：
Essen, Lars-Oliver
中科院分区：
文献类型：
--
作者：
Kiontke, Stephan;Geisselbrecht, Yann;Essen, Lars-Oliver
II 类光裂合酶普遍存在于植物、动物、原核生物和一些病毒中。与远缘微生物 I 类光裂合酶一样，这些酶使用蓝光/近紫外光修复双链 DNA 内紫外线诱导的环丁烷嘧啶二聚体 (CPD) 损伤。 Methanosarcina mazei Mm0852 是甲烷八叠球菌目的 II 类光裂合酶，与植物和后生动物的对应物密切相关。 Mm0852 催化光驱动的 DNA 修复和光还原，但与 I 类酶相比，它缺乏紫外线损伤和完整双链 DNA 之间的高度结合区分。我们解析了 Mm0852 的晶体结构，这是第一个 II 类光裂合酶的晶体结构，单独以及与含有 CPD 损伤的双链 DNA 形成复合物。损伤结合模式与其他光裂合酶的不同之处在于具有更大的 DNA 结合位点，并且发现未修复的 CPD 损伤翻转到活性位点，并被结合的 30-胸腺嘧啶碱基旁边的五个水分子簇识别。与光裂合酶-隐色素家族的其他成员不同，II 类光裂合酶似乎利用一种不寻常的、保守的色氨酸二联体作为催化 FAD 辅因子的电子转移途径。 EMBO 杂志 (2011) 30, 4437-4449。 doi：10.1038/emboj.2011.313； 2011 年 9 月 2 日在线发布
Class II photolyases ubiquitously occur in plants, animals, prokaryotes and some viruses. Like the distantly related microbial class I photolyases, these enzymes repair UV-induced cyclobutane pyrimidine dimer (CPD) lesions within duplex DNA using blue/near-UV light. Methanosarcina mazei Mm0852 is a class II photolyase of the archaeal order of Methanosarcinales, and is closely related to plant and metazoan counterparts. Mm0852 catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA. We solved crystal structures of Mm0852, the first one for a class II photolyase, alone and in complex with CPD lesion-containing duplex DNA. The lesion-binding mode differs from other photolyases by a larger DNA-binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 30-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophane dyad as electron transfer pathway to the catalytic FAD cofactor. The EMBO Journal (2011) 30, 4437-4449. doi:10.1038/emboj.2011.313; Published online 2 September 2011