尿嘧啶-DNA糖基化酶进行特异性碱基切除修复的结构基础。
The structural basis of specific base-excision repair by uracil-DNA glycosylase.
作者信息
Savva R, McAuley-Hecht K, Brown T, Pearl L
机构信息
Department of Biochemistry and Molecular Biology, University College London, UK.
出版信息
Nature. 1995 Feb 9;373(6514):487-93. doi: 10.1038/373487a0.
The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision.
1型单纯疱疹病毒尿嘧啶-DNA糖基化酶的1.75埃晶体结构揭示了一种与二核苷酸结合蛋白有远亲关系的新折叠结构。与三脱氧核苷酸和尿嘧啶形成的复合物确定了DNA结合位点，并有助于详细了解对DNA中尿嘧啶的高度特异性识别。整体结构提示了针对延长的单链和双链DNA底物的结合模型。靠近尿嘧啶结合位点的保守残基提示了水解碱基切除的催化机制。
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