• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the Escherichia coli RNA polymerase alpha subunit C-terminal domain.
【24h】

Structure of the Escherichia coli RNA polymerase alpha subunit C-terminal domain.

机译：大肠杆菌RNA聚合酶的结构α亚基c端域。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The alpha subunit C-terminal domain (alphaCTD) of RNA polymerase (RNAP) is a key element in transcription activation in Escherichia coli, possessing determinants responsible for the interaction of RNAP with DNA and with transcription factors. Here, the crystal structure of E. coli alphaCTD (alpha subunit residues 245-329) determined to 2.0 A resolution is reported. Crystals were obtained after reductive methylation of the recombinantly expressed domain. The crystals belonged to space group P2(1) and possessed both pseudo-translational symmetry and pseudo-merohedral twinning. The refined coordinate model (R factor = 0.193, R(free) = 0.236) has improved geometry compared with prior lower resolution determinations of the alphaCTD structure [Jeon et al. (1995), Science, 270, 1495-1497; Benoff et al. (2002), Science, 297, 1562-1566]. An extensive dimerization interface formed primarily by N- and C-terminal residues is also observed. The new coordinates will facilitate the improved modeling of alphaCTD-containing multi-component complexes visualized at lower resolution using X-ray crystallography and electron-microscopy reconstruction.
机译：α亚基c端域(alphaCTD)RNA聚合酶(RNAP)是一个关键因素转录激活在大肠杆菌中,拥有负责决定因素RNAP DNA和交互转录因子。大肠杆菌alphaCTD(α亚基的结构残留分辨率2.0 245 - 329)的决心据报道。还原甲基化的重组表示域。P2(1)和拥有pseudo-translational对称和pseudo-merohedral孪生。协调模型(R因子= 0.193,=(免费)0.236)改善了几何与之前相比低分辨率alphaCTD的决定结构(全et al。(1995),科学,270,1495-1497;1562 - 1566年)。形成主要由N - c端残留也观察到。方便的改进模型alphaCTD-containing多组分的复合物低分辨率可视化使用x射线晶体学和电子显微镜重建。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号