• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray analysis of the ATPase domain of the sigma(54)-dependent transcription activator NtrC1 from Aquifex aeolicus bound to the ATP analog ADP-BeFx
【24h】

Crystallization and preliminary X-ray analysis of the ATPase domain of the sigma(54)-dependent transcription activator NtrC1 from Aquifex aeolicus bound to the ATP analog ADP-BeFx

机译：Aquifex aeolicus依赖于ATP类似物ADP-BeFx的sigma（54）依赖性转录激活因子NtrC1的ATPase域的结晶和初步X射线分析

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

One way that bacteria regulate the transcription of specific genes to adapt to environmental challenges is to use different sigma factors that direct the RNA polymerase holoenzyme to distinct promoters. Unlike sigma(70) RNA polymerase (RNAP), sigma(54) RNAP is unable to initiate transcription without an activator: enhancer-binding protein (EBP). All EBPs contain one ATPase domain that belongs to the family of ATPases associated with various cellular activities (AAA+ ATPases). AAA+ ATPases use the energy of ATP hydrolysis to remodel different target macromolecules to perform distinct functions. These mechanochemical enzymes are known to form ring-shaped oligomers whose conformations strongly depend upon nucleotide status. Here, the crystallization of the AAA+ ATPase domain of an EBP from Aquifex aeolicus, NtrC1, in the presence of the non-hydrolyzable ATP analog ADP-BeFx is reported. X-ray diffraction data were collected from two crystals from two different protein fractions of the NtrC1 ATPase domain. Previously, this domain was co-crystallized with ADP and ATP, but the latter crystals were grown from the Walker B substitution variant E239A. Therefore, the new data sets are the first for a wild-type EBP ATPase domain co-crystallized with an ATP analog and they reveal a new crystal form. The resulting structure(s) will shed light on the mechanism of EBP-type transcription activators.
机译：细菌调节特定基因的转录以适应环境挑战的一种方法是使用不同的sigma因子来指导RNA聚合酶全酶到达不同的启动子。与sigma（70）RNA聚合酶（RNAP）不同，sigma（54）RNAP在没有激活剂：增强子结合蛋白（EBP）的情况下无法启动转录。所有EBP都包含一个ATPase域，该域属于与各种细胞活动相关的ATPase家族（AAA + ATPase）。 AAA + ATPases利用ATP水解的能量来重构不同的目标大分子以执行不同的功能。已知这些机械化学酶形成环状寡聚体，其构象强烈取决于核苷酸状态。在此，报道了在不可水解的ATP类似物ADP-BeFx存在下，来自Aquifex aeolicus NtrC1的EBP的AAA + ATPase结构域的结晶。 X射线衍射数据是从NtrC1 ATPase域的两个不同蛋白质部分的两个晶体中收集的。以前，此结构域与ADP和ATP共结晶，但后者晶体是从Walker B替代变体E239A生长的。因此，新数据集是第一个与ATP类似物共结晶的野生型EBP ATPase域的数据集，它们揭示了一种新的晶体形式。最终的结构将阐明EBP型转录激活因子的机制。

著录项

相似文献

  • 外文文献
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