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炭疽杆菌转录阻遏蛋白 PagR 的晶体结构。

Crystal structure of the transcriptional repressor PagR of Bacillus anthracis.

机构信息

Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.

Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, 4301 W Markham St, Little Rock, AR 72205-7199, USA.

出版信息

Microbiology (Reading). 2010 Feb;156(Pt 2):385-391. doi: 10.1099/mic.0.033548-0. Epub 2009 Nov 19.

Abstract

PagR is a transcriptional repressor in Bacillus anthracis that controls the chromosomal S-layer genes eag and sap, and downregulates the protective antigen pagA gene by direct binding to their promoter regions. The PagR protein sequence is similar to those of members of the ArsR repressor family involved in the repression of arsenate-resistance genes in numerous bacteria. The crystal structure of PagR was solved using multi-wavelength anomalous diffraction (MAD) techniques and was refined with 1.8 A resolution diffraction data. The PagR molecules form dimers, as observed in all SmtB/ArsR repressor family proteins. In the crystal lattice four PagR dimers pack together to form an inactive octamer. Model-building studies suggest that the dimer binds to a DNA duplex with a bend of around 4 degrees.

摘要

PagR 是炭疽芽胞杆菌中的一种转录阻遏物,它控制着染色体 S 层基因 eag 和 sap,并通过直接结合它们的启动子区域下调保护性抗原 pagA 基因。PagR 蛋白序列与参与许多细菌中砷酸盐抗性基因抑制的 ArsR 阻遏物家族成员的序列相似。使用多波长异常衍射 (MAD) 技术解决 PagR 的晶体结构,并使用 1.8A 分辨率衍射数据进行了细化。如在所有 SmtB/ArsR 阻遏物家族蛋白中观察到的那样,PagR 分子形成二聚体。在晶格中,四个 PagR 二聚体聚集在一起形成无活性的八聚体。模型构建研究表明,二聚体与具有约 4 度弯曲的 DNA 双链结合。

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