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	Crystal structure of the coxsackievirus a16 rna-dependent rna polymerase elongation complex reveals novel features in motif a dynamics
	Bi, Peng1,2; Shu, Bo1,2; Gong, Peng1
刊名	Virologica sinica
	2017-12-01
卷号	32期号:6页码:548-552
ISSN号	1674-0769
DOI	10.1007/s12250-017-4066-8
通讯作者	Gong, peng(gongpeng@wh.iov.cn)
英文摘要	The rna-dependent rna polymerases (rdrps) encoded by rna viruses represent a unique class of nucleic acid polymerases. unlike other classes of single-subunit polymerases, viral rdrps have evolved a unique conformational change in their palm domain to close the active site during catalysis. the hallmark of this conformational change is the backbone shift of the polymerase motif a from an "open" state to a "closed" state, allowing two universally conserved aspartic acid residues to orient toward each other for divalent metal binding and catalysis. the "closed" motif a conformation was only observed upon the binding of correct ntp in rdrp catalytic complexes or under rare conditions such as induced by a bound lutetium ion or a bound glutamate molecule. by solving the crystal structure of the catalytic elongation complex of the coxsackievirus rdrp, we in this work observed for the first time the "closed" motif a conformation in the absence of an ntp substrate or other conformational-change-inducing factors. this observation emphasizes the intrinsic dynamic features of viral rdrp motif a, and solidifies the structural basis for how this important structural element participates in catalytic events of the rdrps.
WOS关键词	ACTIVE-SITE ; TRANSLOCATION ; CATALYSIS
WOS研究方向	Virology
WOS类目	Virology
语种	英语
出版者	SPRINGER
WOS记录号	WOS:000419186700014
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2373352
专题	武汉病毒研究所
通讯作者	Gong, Peng
作者单位	1.Chinese Acad Sci, Wuhan Inst Virol, Key Lab Special Pathogens & Biosafety, Wuhan 430071, Hubei, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Bi, Peng,Shu, Bo,Gong, Peng. Crystal structure of the coxsackievirus a16 rna-dependent rna polymerase elongation complex reveals novel features in motif a dynamics[J]. Virologica sinica,2017,32(6):548-552.
APA	Bi, Peng,Shu, Bo,&Gong, Peng.(2017).Crystal structure of the coxsackievirus a16 rna-dependent rna polymerase elongation complex reveals novel features in motif a dynamics.Virologica sinica,32(6),548-552.
MLA	Bi, Peng,et al."Crystal structure of the coxsackievirus a16 rna-dependent rna polymerase elongation complex reveals novel features in motif a dynamics".Virologica sinica 32.6(2017):548-552.

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