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题名: F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations
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
学科分类: Chemistry
DOI: http://dx.doi.org/10.3866/PKU.WHXB201508062
通讯作者: Wu, SG (reprint author), Sichuan Normal Univ, Coll Chem & Mat Sci, Chengdu 610068, Peoples R China.
文章类型: Article
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.
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
项目资助者: National Natural Science Foundation of China [11405113] ;  Science and Technology Plan of Sichuan Province, China [2010JY0122] ;  Science Research Fund of Sichuan Normal University, China [10MSL02]
语种: 中文
Citation statistics: 
内容类型: 期刊论文
URI标识: http://ir.itp.ac.cn/handle/311006/20880
Appears in Collections:理论物理所2015年知识产出_期刊论文

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Recommended Citation:
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.
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