Structure of a replication-terminator protein complexed with DNA

被引：92

作者：

Kamada, K

Horiuchi, T

Ohsumi, K

Shimamoto, N

Morikawa, K

机构：

[1] PROT ENGN RES INST,BIOMOL ENGN RES INST,SUITA,OSAKA 565,JAPAN

[2] NATL INST GENET,MISHIMA,SHIZUOKA 411,JAPAN

[3] GRAD UNIV ADV STUDIES,DEPT MOL BIOMECH,OKAZAKI,AICHI 444,JAPAN

[4] NATL INST BASIC BIOL,OKAZAKI,AICHI 444,JAPAN

[5] GRAD UNIV ADV STUDIES,DEPT GENET,MISHIMA,SHIZUOKA 411,JAPAN

来源：

NATURE | 1996年 / 383卷 / 6601期

关键词：

D O I：

10.1038/383598a0

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 the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 Angstrom resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain beta-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.

引用

页码：598 / 603

页数：6

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