期刊
BIOCHEMISTRY
卷 49, 期 10, 页码 2205-2215出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi902133s
关键词
-
资金
- NIH [T90-DK070076, 1-U54-Al-057153]
- Arnold and Mabel Beckman Foundation
- Mallinckrodt Foundation
- NIH-NIAID
Toxin-antitoxin (TA) systems form it ubiquitous class of prokaryotic proteins with functional roles in plasmid inheritance, environmental stress response, and cell development. ParDE family TA systems are broadly conserved oil plasmids and bacterial chromosomes and have been well characterized as genetic elements that promote stable plasmid Inheritance. We present a crystal structure of a chromosomally encoded ParD-ParE complex from Caulobacter crescentus at 2.6 angstrom resolution. This TA system forms an alpha(2)beta(2) heterotetramer in the crystal and in solution. The toxin-antitoxin binding interface reveals extensive polar and hydrophobic contacts of ParD antitoxin helices with a conserved recognition and binding groove oil the ParE toxin. A cross-species comparison of this complex structure with related toxin structures identified all antitoxin recognition and binding subdomain that is conserved between distantly related members of the RelE/ParE toxin superfamily despite a low level of overall primary sequence identify. We further demonstrate that ParD antitoxin is dimeric, stably folded, and largely helical when not bound to ParE toxin. Thus, the paradigmatic model in which antitoxin Undergoes I disorder-to-order transition upon toxin binding does not apply to this chromosomal ParD-ParE TA system.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据