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	Dynamic mechanism for the autophosphorylation of chea histidine kinase: molecular dynamics simulations
	Zhang, J; Xu, YC; Shen, JH; Luo, XM; Chen, JG; Chen, KX; Zhu, WL; Jiang, HL
刊名	Journal of the american chemical society
	2005-08-24
卷号	127期号:33页码:11709-11719
ISSN号	0002-7863
DOI	10.1021/ja051199o
通讯作者	Zhu, wl()
英文摘要	The two-component system (tcs) is an important signal transduction component for most bacteria. this signaling pathway is mediated by histidine kinases via autophosphorylation between p1 and p4 domains. taking chemotaxis protein chea as a model of tcs, the autophosphorylation mechanism of the tcs histidine kinases has been investigated in this study by using a computational approach integrated homology modeling, ligand-protein docking, protein-protein docking, and molecular dynamics (md) simulations. four nanosecond-scale mid simulations were performed on the free p4 domain, p4-atp, p4-tnpatp, and p1-p4-atp complexes, respectively. upon its binding to the binding pocket of p4 with a folded conformation, atp gradually extends to an open state with help from a water molecule. meanwhile, atp forms two hydrogen bonds with his413 and lys494 at this state. because of the lower energy of the folded conformations, atp shrinks back to its folded conformations, leading to the rupture of the hydrogen bond between atp and lys494. consequently, lys494 moves away from the pocket entrance, resulting in an open of the atp lid of p4. it is the open state of p4 that can bind tightly to p1, where the his45 of p1 occupies a favorable position for its autophosphorylation from atp. this indicates that atip is not only a phosphoryl group donor but also an activator for chea phosphorylation. accordingly, a mechanism of the autophosphorylation of chea is proposed as that the atp conformational switch triggers the opening of the atp lid of p4, leading to p1 binding tightly, and subsequently autophosphorylation from atp to p1.
WOS关键词	2-COMPONENT SIGNAL-TRANSDUCTION ; BACTERIAL CHEMOTAXIS ; ESCHERICHIA-COLI ; PROTEIN-KINASE ; DOMAIN MOTIONS ; ORBITAL ELECTRONEGATIVITY ; CONFORMATIONAL-CHANGE ; NUCLEOTIDE-BINDING ; PHOSPHORYLATION ; ACTIVATION
WOS研究方向	Chemistry
WOS类目	Chemistry, Multidisciplinary
语种	英语
出版者	AMER CHEMICAL SOC
WOS记录号	WOS:000231454100056
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2377634
专题	中国科学院大学
通讯作者	Zhu, WL
作者单位	1.Chinese Acad Sci, State Key Lab Drug Res, Shanghai Inst Mat Med, Ctr Drug Discovery & Design,Shanghai Inst Biol Sc, Shanghai 201203, Peoples R China 2.Chinese Acad Sci, Grad Sch, Shanghai 201203, Peoples R China 3.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China
推荐引用方式 GB/T 7714	Zhang, J,Xu, YC,Shen, JH,et al. Dynamic mechanism for the autophosphorylation of chea histidine kinase: molecular dynamics simulations[J]. Journal of the american chemical society,2005,127(33):11709-11719.
APA	Zhang, J.,Xu, YC.,Shen, JH.,Luo, XM.,Chen, JG.,...&Jiang, HL.(2005).Dynamic mechanism for the autophosphorylation of chea histidine kinase: molecular dynamics simulations.Journal of the american chemical society,127(33),11709-11719.
MLA	Zhang, J,et al."Dynamic mechanism for the autophosphorylation of chea histidine kinase: molecular dynamics simulations".Journal of the american chemical society 127.33(2005):11709-11719.

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