Preliminary crystallographic analysis of the Escherichia coli antitoxin MqsA (YgiT/b3021) in complex with mqsRA promoter DNA

被引：5

作者：

Brown, Breann L. ^{[2
]}

Page, Rebecca ^{[1
]}

机构：

[1] Brown Univ, Dept Mol Biol Cell Biol & Biochem, Providence, RI 02912 USA

[2] Brown Univ, Dept Mol Pharmacol Physiol & Biotechnol, Providence, RI 02912 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

MqsA; Escherichia coli; DNA-binding proteins; antitoxins; protein-DNA complexes; CRYSTAL-STRUCTURE; MULTIDRUG TOLERANCE; TOXIN; MECHANISM;

D O I：

10.1107/S1744309110028617

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The Escherichia coli proteins MqsR and MqsA comprise a novel toxin-antitoxin (TA) system. MqsA, the antitoxin, defines a new family of antitoxins because unlike other antitoxins MqsA is structured throughout its entire sequence, binds zinc and coordinates DNA via its C-terminal and not its N-terminal domain. In order to understand how bacterial antitoxins, and MqsA in particular, regulate transcription, the MqsA protein was cocrystallized with a 26-mer duplex DNA corresponding to the palindromic region of the mqsRA promoter. The merohedrally twinned crystal belonged to space group P4(1), with unit-cell parameters a = 60.99, b = 60.99, c = 148.60 A. A complete data set was collected to a resolution of 2.1 A. The solvent content of the crystal was consistent with the presence of two MqsA molecules bound to the duplex DNA in the asymmetric unit.

引用

页码：1060 / 1063

页数：4