Structure of tRNA-Modifying Enzyme TiaS and Motions of Its Substrate Binding Zinc Ribbon

doi:10.1016/j.jmb.2018.08.015

	Structure of tRNA-Modifying Enzyme TiaS and Motions of Its Substrate Binding Zinc Ribbon
	Li, Fahui; Gao, Feng; Wei, Jia; Lin, Yajing; Zhang, Yong; Lou, Jizhong; Liu, Guangfeng; Dong, Yuhui; Liu, Lin; Wang, Jiangyun
刊名	JOURNAL OF MOLECULAR BIOLOGY
	2018
卷号	430 期号:21 页码:4183-4194
关键词	zinc finger conformational change tRNA modification catalytic mechanism
ISSN号	0022-2836
DOI	10.1016/j.jmb.2018.08.015
文献子类	Article
英文摘要	The accurate modification of the tRNA(lie) anticodon wobble cytosine 34 is critical for AUA decoding in protein synthesis. Archaeal tRNA(lle2) cytosine 34 is modified with agmatine in the presence of ATP by TiaS (tRNA(lle2) agmatidine synthetase). However, no structure of apo-form full-length TiaS is available currently. Here, the crystal structures of apo TiaS and a complex of TiaS agmatine AMPPCP Mg, are presented, with properly folded zinc ribbon and Cys4-zinc coordination identified. Compared with tRNA(lle)-bound form, the architecture of apo TiaS shows a totally different conformation of zinc ribbon. Molecular dynamics simulations of the docking complex between free-state TiaS and tRNA(lle2) suggest that zinc ribbon domain is capable of performing large-scale motions to sample substrate binding-competent conformation. Principle component analysis and normal mode analysis show consistent results about the relative directionality of functionally correlated zinc ribbon motions. Apo TiaS and TiaS-agmatine-AMPPCP-Mg/TiaS-AMPCPP-Mg complex structures capture two snapshots of the flexible ATP-Mg binding p2loop step-by-step stabilization. Research from this study provides new insight into TiaS functional mechanism and the dynamic feature of zinc ribbons. (C) 2018 Elsevier Ltd. All rights reserved.
电子版国际标准刊号	1089-8638
WOS关键词	AMINO-ACID SPECIFICITIES ; ISOLEUCINE TRANSFER-RNA ; FINGER DNA RECOGNITION ; AUA CODON ; LYSIDINE SYNTHETASE ; PROTEIN STRUCTURES ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; ANTICODON ; CYTIDINE
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
WOS记录号	WOS:000448493400022
内容类型	期刊论文
源URL	[http://ir.ihep.ac.cn/handle/311005/286656]
专题	高能物理研究所_多学科研究中心高能物理研究所_粒子天体物理中心高能物理研究所_核技术应用研究中心
作者单位	中国科学院高能物理研究所
推荐引用方式 GB/T 7714	Li, Fahui,Gao, Feng,Wei, Jia,et al. Structure of tRNA-Modifying Enzyme TiaS and Motions of Its Substrate Binding Zinc Ribbon[J]. JOURNAL OF MOLECULAR BIOLOGY,2018,430(21):4183-4194.
APA	Li, Fahui.,Gao, Feng.,Wei, Jia.,Lin, Yajing.,Zhang, Yong.,...&Dong, Jianshu.(2018).Structure of tRNA-Modifying Enzyme TiaS and Motions of Its Substrate Binding Zinc Ribbon.JOURNAL OF MOLECULAR BIOLOGY,430(21),4183-4194.
MLA	Li, Fahui,et al."Structure of tRNA-Modifying Enzyme TiaS and Motions of Its Substrate Binding Zinc Ribbon".JOURNAL OF MOLECULAR BIOLOGY 430.21(2018):4183-4194.