Structure and mechanism of DNA topoisomerase II

被引：740

作者：

Berger, JM

Gamblin, SJ

Harrison, SC

Wang, JC

机构：

[1] HARVARD UNIV,DEPT MOLEC & CELLULAR BIOL,CAMBRIDGE,MA 02138

[2] HARVARD UNIV,HOWARD HUGHES MED INST,CAMBRIDGE,MA 02138

来源：

NATURE | 1996年 / 379卷 / 6562期

关键词：

D O I：

10.1038/379225a0

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 crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints. An enzyme with bound DNA can admit a second DNA duplex through one set of jaws, transport it through the cleaved first duplex, and expel it through the other set of jaws.

引用

页码：225 / 232

页数：8

共 43 条

[1] DNA-SEQUENCE AND TRANSCRIPTION OF THE REGION UPSTREAM OF THE ESCHERICHIA-COLI GYRB-GENE [J].