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

被引：355

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

页码：487 / 493

页数：7

共 38 条

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