Knowledge Management System of Institute of Theoretical Physics, CAS
| Wu, SG; Gao, XT; Li, Q; Liao, J; Xu, CG; Wu, SG (reprint author), Sichuan Normal Univ, Coll Chem & Mat Sci, Chengdu 610068, Peoples R China. | |
| F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations | |
| Source Publication | ACTA PHYSICO-CHIMICA SINICA
 |
| Language | 中文 |
| Keyword | F-1-atpase Hydrogen Bond Molecular Dynamics Mutation |
| Abstract | 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. |
| 2015 | |
| Volume | 31Issue:9Pages:1803-1809 |
| Subject Area | Chemistry |
| DOI | http://dx.doi.org/10.3866/PKU.WHXB201508062 |
| Indexed By | SCI |
| Funding Organization | National Natural Science Foundation of China [11405113] ; National Natural Science Foundation of China [11405113] ; National Natural Science Foundation of China [11405113] ; National Natural Science Foundation of China [11405113] ; Science and Technology Plan of Sichuan Province, China [2010JY0122] ; Science and Technology Plan of Sichuan Province, China [2010JY0122] ; Science and Technology Plan of Sichuan Province, China [2010JY0122] ; Science and Technology Plan of Sichuan Province, China [2010JY0122] ; Science Research Fund of Sichuan Normal University, China [10MSL02] ; Science Research Fund of Sichuan Normal University, China [10MSL02] ; Science Research Fund of Sichuan Normal University, China [10MSL02] ; Science Research Fund of Sichuan Normal University, China [10MSL02] |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.itp.ac.cn/handle/311006/20880 |
| Collection | SCI期刊论文 |
| Corresponding Author | Wu, SG (reprint author), Sichuan Normal Univ, Coll Chem & Mat Sci, Chengdu 610068, Peoples R China. |
| Recommended Citation 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,&Wu, SG .(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. |
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| File Name/Size | DocType | Version | Access | License | ||
| F-1-ATPase Stabilize（3700KB） | 期刊论文 | 出版稿 | 开放获取 | CC BY-NC-SA | Application Full Text | |
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