Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus
Crystal structure of the DNA nucleotide excision repair enzyme UvrB from Thermus thermophilus
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DOI：
10.1073/pnas.96.21.11717
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发表时间：
1999-10-12
影响因子：
11.1
通讯作者：
Deisenhofer, J
中科院分区：
文献类型：
--
作者：
Machius, M;Henry, L;Deisenhofer, J
核苷酸切除修复(NER)是生物体内最重要的DNA修复机制。在原核生物中，形成UvrABC系统的三种酶启动了各种结构上不同的DNA损伤的NER。UvrB是该系统的中心组成部分，负责最终的DNA损伤识别，并参与损伤DNA链的切割。Thermos thermophilus UvrB的晶体结构揭示了一个核心，该核心在结构上类似于解旋酶中的CARE区域，在那里它们构成分子马达。与DNA结合的其他结构域和NER系统的各种成分都附着在这个中央核心上。DNA结合位点的结构和分布为DNA损伤识别过程提供了一个可能的模型。
Nucleotide excision repair (NER) is the most important DNA-repair mechanism in living organisms. In prokaryotes, three enzymes forming the UvrABC system initiate NER of a variety of structurally different DNA lesions. UvrB, the central component of this system, is responsible for the ultimate DNA damage recognition and participates in the incision of the damaged DNA strand. The crystal structure of Thermos thermophilus UvrB reveals a core that is structurally similar to care regions found in helicases, where they constitute molecular motors. Additional domains implicated in binding to DNA and various components of the NER system are attached to this central core. The architecture and distribution of DNA binding sites suggest a possible model for the DNA damage recognition process.