大肠杆菌YafN-YafO络合物的结晶及初步结晶学研究。

IF 0.9 4区 生物学
Fan Zhang, Li Xing, Maikun Teng, Xu Li
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引用次数: 2

摘要

来自大肠杆菌的核糖体依赖性mRNA干扰酶YafO属于II型毒素-抗毒素(TA)系统,其同源抗毒素YafN通过形成稳定的YafN-YafO复合物来中和细胞毒性。YafN-YafO TA系统通过SOS反应(一种对DNA损伤的全局反应,其中细胞周期被阻止并诱导突变)上调,然后可能通过YafO与50S核糖体亚基的核糖核酸内酶活性抑制蛋白质合成。YafN-YafO复合物及其相关复合物的结构信息将有助于了解mRNA识别和切割机制的结构基础,以及这些复合物的组装。在这里,YafN-YafO复合物被表达和结晶。悬垂气相扩散法生长的晶体衍射分辨率为3.50 Å,属于六边形空间群P622,晶胞参数为a = 86.14, b = 86.14, c = 173.11 Å, α = β = 90, γ = 120°。Matthews系数分析和自旋函数表明,晶体中每个不对称单元存在1个分子,溶剂含量为65.69% (V(M) = 3.58 Å(3) Da(-1))。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Crystallization and preliminary crystallographic studies of the YafN-YafO complex from Escherichia coli.

Crystallization and preliminary crystallographic studies of the YafN-YafO complex from Escherichia coli.

Crystallization and preliminary crystallographic studies of the YafN-YafO complex from Escherichia coli.

The ribosome-dependent mRNA interferase YafO from Escherichia coli belongs to a type II toxin-antitoxin (TA) system and its cognate antitoxin YafN neutralizes cell toxicity by forming a stable YafN-YafO complex. The YafN-YafO TA system is upregulated by the SOS response (a global response to DNA damage in which the cell cycle is arrested and mutagenesis is induced) and may then inhibit protein synthesis by endoribonuclease activity of YafO with the 50S ribosome subunit. Structural information on the YafN-YafO complex and related complexes would be helpful in order to understand the structural basis of the mechanism of mRNA recognition and cleavage, and the assembly of these complexes. Here, the YafN-YafO complex was expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 3.50 Å resolution and belonged to the hexagonal space group P622, with unit-cell parameters a = 86.14, b = 86.14, c = 173.11 Å, α = β = 90, γ = 120°. Both Matthews coefficient analysis and the self-rotation function suggested the presence of one molecule per asymmetric unit in the crystal, with a solvent content of 65.69% (V(M) = 3.58 Å(3) Da(-1)).

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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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