有哪些信誉好的足球投注网站crystal structure of the dengue virus methyltransferase bound to a 5′-capped octameric rna登革热病毒甲基转移酶的晶体结构绑定到一个5u2032顶部覆octameric rna.pdfVIP
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crystal structure of the dengue virus methyltransferase bound to a 5′-capped octameric rna登革热病毒甲基转移酶的晶体结构绑定到一个5u2032顶部覆octameric rna
Crystal Structure of the Dengue Virus Methyltransferase Bound to a 59-Capped Octameric RNA 1,2 1 1,2 2 2 Li Jian Yap , Dahai Luo , Ka Yan Chung , Siew Pheng Lim , Christophe Bodenreider , Christian 2 2 1,3 Noble , Pei-Yong Shi *, Julien Lescar * 1 School of Biological Sciences, Nanyang Technological University, Singapore, Singapore, 2 Novartis Institute for Tropical Diseases, Singapore, Singapore, 3 AFMB UMR6098 CNRS, Marseille, France Abstract The N-terminal domain of the flavivirus NS5 protein functions as a methyltransferase (MTase). It sequentially methylates the N7 and 29-O positions of the viral RNA cap structure (GpppAR7meGpppAR7meGpppA29-O-me). The same NS5 domain could also have a guanylyltransferase activity (GTP+ppA-RNARGpppA). The mechanism by which this protein domain catalyzes these three distinct functions is currently unknown. Here we report the crystallographic structure of DENV-3 MTase in ˚ complex with a 59-capped RNA octamer (GpppAGAACCUG) at a resolution of 2.9 A. Two RNA octamers arranged as kissing loops are encircled by four MTase monomers around a 2-fold non-crystallography symmetry axis. Only two of the four monomers make direct contact with the 59 end of RNA. The RNA structure is stabilised by the formation of several intra and intermolecular base stacking and non-canonical base pairs. The structure may represent the product of guanylylation of the viral genome prior to the subsequent methylation events that require repositioning of the RNA substrate to reach to the methyl-donor site
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