F-1-ATPase Stabilizes and Positions Adenosine Triphosphate Revealed by Molecular Dynamics Simulations

doi:http://dx.doi.org/10.3866/PKU.WHXB201508062

ITP OpenIR > 理论物理所科研产出 > SCI论文

	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
发表期刊	ACTA PHYSICO-CHIMICA SINICA
语种	中文
关键词	F-1-atpase Hydrogen Bond Molecular Dynamics Mutation
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.
	2015
卷号	31 期号:9 页码:1803-1809
学科领域	Chemistry
DOI	http://dx.doi.org/10.3866/PKU.WHXB201508062
收录类别	SCI
项目资助者	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]
引用统计
文献类型	期刊论文
条目标识符	http://ir.itp.ac.cn/handle/311006/20880
专题	理论物理所科研产出_SCI论文
通讯作者	Wu, SG (reprint author), Sichuan Normal Univ, Coll Chem & Mat Sci, Chengdu 610068, Peoples R China.
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,&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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