Structure of a DNA glycosylase searching for lesions

被引：167

作者：

Banerjee, A

Santos, WL

Verdine, GL ^{[1
]}

机构：

[1] Harvard Univ, Dept Chem & Biol Chem, Cambridge, MA 02138 USA

[2] Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA

来源：

SCIENCE | 2006年 / 311卷 / 5764期

关键词：

D O I：

10.1126/science.1120288

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：

DNA glycosylases must interrogate millions of base pairs of undamaged DNA in order to locate and then excise one damaged nucleobase. The nature of this search process remains poorly understood. Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial. DNA glycosylase, MutM, interrogating undamaged DNA. These structures, solved to 2.0 angstrom resolution, reveal the nature of the search process: The protein inserts a probe residue into the helical stack and severely buckles the target base pair, which remains intrahelical. MutM therefore actively interrogates the intact DNA helix white searching for damage.

引用

页码：1153 / 1157

页数：5

共 32 条

[1] STUDIES ON PHOSPHORYLATION .2. THE REACTION OF DIALKYL PHOSPHITES WITH POLYHALOGEN COMPOUNDS IN PRESENCE OF BASES - A NEW METHOD FOR THE PHOSPHORYLATION OF AMINES [J].