The ParE2-PaaA2 toxin-antitoxin complex from Escherichia coli O157 forms a heterodocecamer in solution and in the crystal.

IF 0.9 4区生物学 Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-25 DOI:10.1107/S1744309112015230

Yann G J Sterckx, Abel Garcia-Pino, Sarah Haesaerts, Thomas Jové, Lieselotte Geerts, Viktor Sakellaris, Laurence Van Melderen, Remy Loris

{"title":"The ParE2-PaaA2 toxin-antitoxin complex from Escherichia coli O157 forms a heterodocecamer in solution and in the crystal.","authors":"Yann G J Sterckx, Abel Garcia-Pino, Sarah Haesaerts, Thomas Jové, Lieselotte Geerts, Viktor Sakellaris, Laurence Van Melderen, Remy Loris","doi":"10.1107/S1744309112015230","DOIUrl":null,"url":null,"abstract":"<p><p>Escherichia coli O157 paaR2-paaA2-parE2 constitutes a unique three-component toxin-antitoxin (TA) module encoding a toxin (ParE2) related to the classic parDE family but with an unrelated antitoxin called PaaA2. The complex between PaaA2 and ParE2 was purified and characterized by analytical gel filtration, dynamic light scattering and small-angle X-ray scattering. It consists of a particle with a radius of gyration of 3.95 nm and is likely to form a heterododecamer. Crystals of the ParE2-PaaA2 complex diffract to 3.8 Å resolution and belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 142.9, c = 87.5 Å. The asymmetric unit is consistent with a particle of around 125 kDa, which is compatible with the solution data. Therefore, the ParE2-PaaA2 complex is the largest toxin-antitoxin complex identified to date and its quaternary arrangement is likely to be of biological significance.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9000,"publicationDate":"2012-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309112015230","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1107/S1744309112015230","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2012/5/25 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 7

Abstract

Escherichia coli O157 paaR2-paaA2-parE2 constitutes a unique three-component toxin-antitoxin (TA) module encoding a toxin (ParE2) related to the classic parDE family but with an unrelated antitoxin called PaaA2. The complex between PaaA2 and ParE2 was purified and characterized by analytical gel filtration, dynamic light scattering and small-angle X-ray scattering. It consists of a particle with a radius of gyration of 3.95 nm and is likely to form a heterododecamer. Crystals of the ParE2-PaaA2 complex diffract to 3.8 Å resolution and belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 142.9, c = 87.5 Å. The asymmetric unit is consistent with a particle of around 125 kDa, which is compatible with the solution data. Therefore, the ParE2-PaaA2 complex is the largest toxin-antitoxin complex identified to date and its quaternary arrangement is likely to be of biological significance.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

来自大肠杆菌O157的ParE2-PaaA2毒素-抗毒素复合物在溶液和晶体中形成异docecamer。

大肠杆菌O157 paaR2-paaA2-parE2构成了一个独特的三组分毒素-抗毒素（TA）模块，编码一种与经典parDE家族有关但与一种名为paaA2的无关抗毒素有关的毒素（parE2）。纯化了PaaA2和ParE2的配合物，并通过分析凝胶过滤、动态光散射和小角度X射线散射对其进行了表征。它由回转半径为3.95nm的粒子组成，很可能形成异十二碳星。ParE2-PaaA2复合物的晶体衍射至3.8Å分辨率，属于空间群P3（1）21或P3（2）21，晶胞参数a=b=142.9，c=87.5Å。不对称单元与大约125kDa的颗粒一致，这与溶液数据兼容。因此，ParE2-PaaA2复合物是迄今为止鉴定的最大的毒素-抗毒素复合物，其四元排列可能具有生物学意义。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Acta Crystallographica Section F-structural Biology and Crystallization Communications 生物-晶体学

自引率

0.00%

发文量

审稿时长

2-4 weeks

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.