| 分子伴侣HdeA与底物蛋白SurA作用机制的模拟研究 |
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| 引用本文： | 周丹丹,于延庆,吴昊,李艳妮,乔建军.分子伴侣HdeA与底物蛋白SurA作用机制的模拟研究[J].生物化学与生物物理进展,2017,44(3):242-252. |
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| 作者姓名： | 周丹丹 于延庆 吴昊 李艳妮 乔建军 |
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| 作者单位： | 天津大学化工学院制药工程系，系统生物工程教育部重点实验室，天津 300072,上海药明康德新药开发有限公司，上海 200131,天津大学化工学院制药工程系，系统生物工程教育部重点实验室，天津 300072,天津大学化工学院制药工程系，系统生物工程教育部重点实验室，天津 300072,天津大学化工学院制药工程系，系统生物工程教育部重点实验室，天津 300072 |
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| 基金项目： | 国家自然科学基金(31570049)资助项目 |
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| 摘 要： | 分子伴侣HdeA与底物蛋白间的相互作用可帮助底物蛋白复性,这是肠道致病菌得以在酸性环境中幸存的重要原因之一.为探究HdeA发挥伴侣活性的作用机制,本研究采用分子对接和分子动力学的方法,模拟了HdeA与底物蛋白SurA间的相互作用,计算了二者的结合自由能.通过分析HdeA-SurA复合物体系的作用模式、氢键作用以及能量分解的结果,确定了HdeA与底物蛋白SurA结合时发挥重要作用的关键氨基酸残基.该研究结果为以后采用实验手段探究HdeA与底物蛋白之间的作用提供了重要的理论参考,同时为今后设计与开发HdeA的抑制剂提供了理论指导依据.
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| 关 键 词： | HdeA，分子伴侣，SurA，分子对接，分子动力学 |
| 收稿时间： | 2016/11/2 0:00:00 |
| 修稿时间： | 2017/2/14 0:00:00 |
Simulation Study on The Mechanism of Molecular Chaperone HdeA and SurA |
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| ZHOU Dan-Dan,YU Yan-Qing,WU Hao,LI Yan-Ni and QIAO Jian-Jun.Simulation Study on The Mechanism of Molecular Chaperone HdeA and SurA[J].Progress In Biochemistry and Biophysics,2017,44(3):242-252. |
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| Authors: | ZHOU Dan-Dan YU Yan-Qing WU Hao LI Yan-Ni and QIAO Jian-Jun |
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| Institution: | Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Key Laboratory of Systems Bioengineering, Ministry of Education, Tianjin 300072, China,WuXi App Tec (Shanghai) Co., Ltd, Shanghai 200131, China,Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Key Laboratory of Systems Bioengineering, Ministry of Education, Tianjin 300072, China,Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Key Laboratory of Systems Bioengineering, Ministry of Education, Tianjin 300072, China and Department of Pharmaceutical Engineering, School of Chemical Engineering and Technology, Tianjin University, Key Laboratory of Systems Bioengineering, Ministry of Education, Tianjin 300072, China |
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| Abstract: | Acid-stress chaperone HdeA and its substrate protein, can contribute to pathogenic-bacteria survival by mutual interactions, when bacteria exposed to extremely acidic conditions. To figure out this mechanisms, molecular docking and molecular dynamics simulation were performed in this paper to investigate the binding mode of SurA to HdeA. MM-PBSA method was used to calculate the binding free energy. The interaction mode, H-bond and energy decompositions of the HdeA-SurA complex were firstly analysed. Based on these analysis, the key amino acid residues which are essential for interactions were subsequently determined. Our results may provide a theoretical guidence for exploring binding mechanism between HdeA and substrate as well as a new strategy for the development of new HdeA inhibitors. |
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| Keywords: | HdeA molecular chaperone SurA molecular docking molecular dynamics |
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