Crystal structure of the transcriptional repressor PagR of Bacillus anthracis.
Crystal structure of the transcriptional repressor PagR of Bacillus anthracis.
复制标题
炭疽杆菌转录抑制子 PagR 的晶体结构。
DOI：
10.1099/mic.0.033548-0
复制
发表时间：
2010
期刊：
影响因子：
--
通讯作者：
Varughese,KottayilI
中科院分区：
文献类型：
--
作者：
Zhao,Haiyan;Volkov,Arsen;Veldore,VidyaHarini;Hoch,JamesA;Varughese,KottayilI
PagR是炭疽芽孢杆菌中的一个转录抑制因子，它控制染色体S层基因的转录，并通过直接与其启动子区结合来下调保护性抗原pagA基因。PagR蛋白序列与参与许多细菌中砷酸盐抗性基因阻遏的ArsR阻遏物家族成员的序列相似。用多波长反常衍射（MAD）技术解析了PagR的晶体结构，并用1.8 nm分辨率的衍射数据进行了修正。 PagR分子形成二聚体，如在所有SmtB/ArsR阻遏物家族蛋白中所观察到的。在晶格中，四个PagR二聚体聚集在一起形成无活性的八聚体。建模研究表明，二聚体与DNA双链体的结合具有约4 °的弯曲。
PagR is a transcriptional repressor inBacillus anthracisthat controls the chromosomal S-layer geneseagandsap, and downregulates the protective antigenpagAgene 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 å 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 °.