• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proteins: Structure, Function, and Genetics >Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation
【24h】

Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation

机译：分子动力学模拟表明，载脂蛋白HisJ可以采样一个封闭的构象

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 Escherichia coli histidine binding protein HisJ is a type II periplasmic binding protein (PBP) that preferentially binds histidine and interacts with its cytoplasmic membrane ABC transporter, HisQMP2, to initiate histidine transport. HisJ is a bilobal protein where the larger Domain 1 is connected to the smaller Domain 2 via two linking strands. Type II PBPs are thought to undergo "Venus flytrap" movements where the protein is able to reversibly transition from an open to a closed conformation. To explore the accessibility of the closed conformation to the apo state of the protein, we performed a set of all-atom molecular dynamics simulations of HisJ starting from four different conformations: apo-open, apo-closed, apo-semiopen, and holo-closed. The simulations reveal that the closed conformation is less dynamic than the open one. HisJ experienced closing motions and explored semiopen conformations that reverted to closed forms resembling those found in the holo-closed state. Essential dynamics analysis of the simulations identified domain closing/opening and twisting as main motions. The formation of specific inter-hinge strand and interdomain polar interactions contributed to the adoption of the closed apo-conformations although they are up to 2.5-fold less prevalent compared with the holo-closed simulations. The overall sampling of the closed form by apo-HisJ provides a rationale for the binding of unliganded PBPs with their cytoplasmic membrane ABC transporters. Proteins 2014; 82:386-398.
机译：大肠杆菌组氨酸结合蛋白HisJ是II型周质结合蛋白（PBP），可优先结合组氨酸并与其胞质膜ABC转运蛋白HisQMP2相互作用，从而开始组氨酸转运。 HisJ是一种双叶蛋白，其中较大的结构域1通过两条连接链连接至较小的结构域2。 II型PBP被认为会经历“维纳斯捕蝇器”运动，其中蛋白质能够从开放构象向封闭构象可逆转变。为了探索封闭构象对蛋白质载脂蛋白状态的可及性，我们从四个不同的构象开始进行了一系列HisH的全原子分子动力学模拟：载脂蛋白开放，载脂蛋白封闭，载脂蛋白半开放和完整关闭。仿真表明，闭合构象比开放构象更不动态。 HisJ经历了闭合运动并探索了半开放构型，该构型恢复为类似于整体闭合状态下的闭合形式。对模拟的基本动力学分析将域的闭合/打开和扭曲确定为主要运动。特定的铰链间链和域间极性相互作用的形成促进了封闭脱辅基构象的采用，尽管与全封闭模拟相比，它们的流行率低了2.5倍。 apo-HisJ对封闭形式的整体采样为未配体的PBPs与它们的细胞质膜ABC转运蛋白结合提供了理论依据。蛋白质2014; 82：386-398。

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