...
首页> 外文期刊>Cell communication & adhesion >Communication of γ Phage Lysin plyG Enzymes Binding toward SrtA for Inhibition of Bacillus Anthracis: Protein–Protein Interaction and Molecular Dynamics Study
【24h】

Communication of γ Phage Lysin plyG Enzymes Binding toward SrtA for Inhibition of Bacillus Anthracis: Protein–Protein Interaction and Molecular Dynamics Study

机译:γ噬菌体溶素plyG酶结合SrtA抑制炭疽芽孢杆菌的交流:蛋白-蛋白质相互作用和分子动力学研究

获取原文
           

摘要

Bacillus anthracis is a pathogenic, Gram-positive bacterium which chiefly affects the livestock of animals and humans through acute disease anthrax. All around the globe this bio-threat organism damages millions of lives in every year and also most of the drugs were not responding properly in inhibition against this diseased pathogen. In recent development, phage therapy is considered as alternative solution to treat this serious infectious disease. In this study, we elucidated the binding of γ phage lysin plyG enzymes toward the SrtA along with its activator peptide LPXTG. Through protein–protein docking and molecular dynamics simulation studies, we showed the distinguished structure complementarity of SrtA and plyG complex. Especially, MD simulation relates strong and stable interaction occurs between the protein complex structures. These results suggest that additional experimental studies on our approach will lead to availability of better inhibitor against the SrtA.
机译:炭疽杆菌是一种致病性革兰氏阳性细菌,主要通过急性疾病炭疽病影响动物和人类的家畜。在全球范围内,这种生物威胁生物每年造成数百万人的生命损失,而且大多数药物在抑制这种病原体方面均没有做出适当的反应。在最近的发展中,噬菌体疗法被认为是治疗这种严重传染病的替代解决方案。在这项研究中,我们阐明了γ噬菌体溶素plyG酶与SrtA及其激活肽LPXTG的结合。通过蛋白质-蛋白质对接和分子动力学模拟研究,我们显示了SrtA和plyG复合物的显着结构互补性。特别地,MD模拟涉及蛋白质复合物结构之间发生强而稳定的相互作用。这些结果表明,关于我们方法的其他实验研究将导致可获得更好的抗SrtA抑制剂。

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