THE STRUCTURAL BASIS OF SPECIFIC BASE-EXCISION REPAIR BY URACIL-DNA GLYCOSYLASE

被引：357
作者：
SAVVA, R
MCAULEYHECHT, K
BROWN, T
PEARL, L
机构：
[1] UCL, DEPT BIOCHEM & MOLEC BIOL, STRUCT BIOCHEM SECT, LONDON WC1E 6BT, ENGLAND
[2] UNIV EDINBURGH, DEPT CHEM, EDINBURGH EH9 3JJ, MIDLOTHIAN, SCOTLAND
来源：
NATURE | 1995年 / 373卷 / 6514期
基金：
英国惠康基金;
关键词：
D O I：
10.1038/373487a0
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The 1.75-Angstrom crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-L 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.
引用
收藏
页码：487 / 493
页数：7
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