Crystal structure of the Murray Valley encephalitis virus NS5 methyltransferase domain in complex with cap analogues

被引：48

作者：

Assenberg, Rene

Ren, Jingshan

Verma, Anil

Walter, Thomas S.

Alderton, David

Hurrelbrink, Robert J.

Fuller, Steephen D.

Bressanelli, Stephane

Owens, Raymond J.

Stuart, David I.

Grimes, Jonathan M.

机构：

[1] Univ Oxford, Henry Wellcome Bldg Genom Med, Oxford Protein Prod Facil, Oxford OX3 7BN, England

[2] Univ Oxford, Henry Wellcome Bldg Genom Med, Div Struct Biol, Oxford OX3 7BN, England

[3] Univ Western Australia, Telethon Inst Child Hlth Res, Dept Virol, Perth, WA 6008, Australia

[4] CNRS, UMR2472, IFR 115, F-91198 Gif Sur Yvette, France

[5] INRA, UMR1157, F-91198 Gif Sur Yvette, France

来源：

JOURNAL OF GENERAL VIROLOGY | 2007年 / 88卷

基金：

英国医学研究理事会;

关键词：

D O I：

10.1099/vir.0.82757-0

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We have determined the high resolution crystal structure of the m ethylt ransfe rase domain of the NS5 polypeptide from the Murray Valley encephalitis virus. This domain is unusual in having both the N7 and 2'-O methyltransferase activity required for Cap 1 synthesis. We have also determined structures for complexes of this domain with nucleoticles and cap analogues providing information on cap binding, based on which we suggest a model of how the sequential methylation of the N7 and 2'-O groups of the cap may be coordinated.

引用

页码：2228 / 2236

页数：9

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