与DNA复合的复制终止蛋白的结构。

Structure of a replication-terminator protein complexed with DNA.

作者信息

Kamada K, Horiuchi T, Ohsumi K, Shimamoto N, Morikawa K

机构信息

Department of Genetics, The Graduate University for Advanced Studies, and National Institute of Genetics, Shizuoka, Japan.

出版信息

Nature. 1996 Oct 17;383(6601):598-603. doi: 10.1038/383598a0.

DOI:10.1038/383598a0

PMID:8857533

Abstract

The crystal structure of the Escherichia coli replication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 A 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.

摘要

已确定大肠杆菌复制终止蛋白（Tus）与终止位点（Ter）DNA结合时的晶体结构，分辨率为2.7埃。Tus蛋白折叠成一种以前未描述过的结构，由一个中央碱性裂隙分为两个结构域。这个裂隙容纳局部变形的B型Ter DNA，并与大沟广泛接触，主要通过两条结构域间的β链。这种复合物不同寻常的结构特征可能解释了复制叉如何仅在一个方向上停止。