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https://doi.org/10.1371/journal.pone.0012836
Title: | Crystal structure of the Dengue virus methyltransferase bound to a 5?-capped octameric RNA | Authors: | Yap L.J. Luo D. Chung K.Y. Lim S.P. Bodenreider C. Noble C. Shi P.-Y. Lescar J. |
Keywords: | adenine capped RNA cytosine guanine methyltransferase monomer protein DENV 3 unclassified drug virus RNA capped RNA methyltransferase virus protein virus RNA 5' untranslated region article base pairing crystal structure crystallography Dengue virus enzyme defect enzyme structure nonhuman protein methylation protein RNA binding RNA stability RNA structure structure analysis virus genome amino acid sequence binding site chemical structure chemistry conformation enzymology genetics metabolism molecular genetics protein binding protein tertiary structure X ray crystallography Dengue virus Flavivirus Amino Acid Sequence Binding Sites Crystallography, X-Ray Dengue Virus Methyltransferases Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Binding Protein Structure, Tertiary RNA Caps RNA, Viral Viral Proteins |
Issue Date: | 2010 | Citation: | Yap L.J., Luo D., Chung K.Y., Lim S.P., Bodenreider C., Noble C., Shi P.-Y., Lescar J. (2010). Crystal structure of the Dengue virus methyltransferase bound to a 5?-capped octameric RNA. PLoS ONE 5 (9) : 1-9. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0012836 | Rights: | Attribution 4.0 International | Abstract: | The N-terminal domain of the flavivirus NS5 protein functions as a methyltransferase (MTase). It sequentially methylates the N7 and 2?-O positions of the viral RNA cap structure (GpppA?7meGpppA?7meGpppA2?-O- me). The same NS5 domain could also have a guanylyltransferase activity (GTP+ppA-RNA?GpppA). 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 5?-capped RNA octamer (GpppAGAACCUG) at a resolution of 2.9 Å. 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 5? 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 sites. The crystal structure provides a structural explanation for the observed trans-complementation of MTases with different methylation defects. © 2010 Yap et al. | Source Title: | PLoS ONE | URI: | https://scholarbank.nus.edu.sg/handle/10635/161807 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0012836 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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