F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations
文献类型：期刊论文
| 作者 | Wu, SG; Gao, XT; Li, Q; Liao, J; Xu, CG |
| 刊名 | ACTA PHYSICO-CHIMICA SINICA
 |
| 出版日期 | 2015 |
| 卷号 | 31期号:9页码:1803-1809 |
| 关键词 | F-1-ATPase Hydrogen bond Molecular dynamics Mutation |
| 通讯作者 | Wu, SG (reprint author), Sichuan Normal Univ, Coll Chem & Mat Sci, Chengdu 610068, Peoples R China. |
| 英文摘要 | F-1-ATPase makes extensive interactions with ATP through forming a network of interactions around ATP. These interactions create a steady environment for ATP synthesis/hydrolysis. Thus understanding these interactions between ATP and F-1-ATPase is essential for understanding ATP synthesis/hydrolysis mechanism. We performed all-atom molecular dynamics (MD) simulations to elucidate these interactions and attempted to identify key residues which play important roles in stabilizing and positioning ATP. By examining the non-bonded energies between ATP and residues of beta(TP) subunit in F-1-ATPase, it is found that residues 158-164, R189, Y345 have significant interactions with ATP. The loop segment (residues 158-164) and R189 surround ATP by a half and they interact with beta and gamma phosphates through forming a network of hydrogen bonds to constraint the motion of ATP triphosphate. The interaction network seals off the conformation of the catalytic site, creating a steady environment for ATP synthesis/hydrolysis. Additionally, ATP base is positioned by the pi-pi stacking interaction from Y345. However, ATP base can slide and move paralleling to the aromatic group of Y345. It is deduced that this motion may facilitate ATP hydrolysis. |
| 学科主题 | Chemistry |
| 类目[WOS] | Chemistry, Physical |
| 关键词[WOS] | BOVINE HEART-MITOCHONDRIA ; PARTICLE MESH EWALD ; FOF1-ATP SYNTHASE ; F0F1-ATP SYNTHASE ; ATP SYNTHASE ; FORCE-FIELD ; MECHANISM ; ROTATION ; SUBUNIT ; PHOSPHORYLATION |
| 收录类别 | SCI |
| 语种 | 中文 |
| 源URL | [http://ir.itp.ac.cn/handle/311006/20880]  |
| 专题 | 理论物理研究所_理论物理所1978-2010年知识产出 |
| 推荐引用方式 GB/T 7714 | Wu, SG,Gao, XT,Li, Q,et al. F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations[J]. ACTA PHYSICO-CHIMICA SINICA,2015,31(9):1803-1809. |
| APA | Wu, SG,Gao, XT,Li, Q,Liao, J,&Xu, CG.(2015).F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations.ACTA PHYSICO-CHIMICA SINICA,31(9),1803-1809. |
| MLA | Wu, SG,et al."F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations".ACTA PHYSICO-CHIMICA SINICA 31.9(2015):1803-1809. |
入库方式： OAI收割
来源：理论物理研究所
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