Please use this identifier to cite or link to this item:
https://doi.org/10.1371/journal.pone.0012836
DC Field | Value | |
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dc.title | Crystal structure of the Dengue virus methyltransferase bound to a 5?-capped octameric RNA | |
dc.contributor.author | Yap L.J. | |
dc.contributor.author | Luo D. | |
dc.contributor.author | Chung K.Y. | |
dc.contributor.author | Lim S.P. | |
dc.contributor.author | Bodenreider C. | |
dc.contributor.author | Noble C. | |
dc.contributor.author | Shi P.-Y. | |
dc.contributor.author | Lescar J. | |
dc.date.accessioned | 2019-11-07T08:01:13Z | |
dc.date.available | 2019-11-07T08:01:13Z | |
dc.date.issued | 2010 | |
dc.identifier.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 | |
dc.identifier.issn | 19326203 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/161807 | |
dc.description.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. | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20191101 | |
dc.subject | adenine | |
dc.subject | capped RNA | |
dc.subject | cytosine | |
dc.subject | guanine | |
dc.subject | methyltransferase | |
dc.subject | monomer | |
dc.subject | protein DENV 3 | |
dc.subject | unclassified drug | |
dc.subject | virus RNA | |
dc.subject | capped RNA | |
dc.subject | methyltransferase | |
dc.subject | virus protein | |
dc.subject | virus RNA | |
dc.subject | 5' untranslated region | |
dc.subject | article | |
dc.subject | base pairing | |
dc.subject | crystal structure | |
dc.subject | crystallography | |
dc.subject | Dengue virus | |
dc.subject | enzyme defect | |
dc.subject | enzyme structure | |
dc.subject | nonhuman | |
dc.subject | protein methylation | |
dc.subject | protein RNA binding | |
dc.subject | RNA stability | |
dc.subject | RNA structure | |
dc.subject | structure analysis | |
dc.subject | virus genome | |
dc.subject | amino acid sequence | |
dc.subject | binding site | |
dc.subject | chemical structure | |
dc.subject | chemistry | |
dc.subject | conformation | |
dc.subject | enzymology | |
dc.subject | genetics | |
dc.subject | metabolism | |
dc.subject | molecular genetics | |
dc.subject | protein binding | |
dc.subject | protein tertiary structure | |
dc.subject | X ray crystallography | |
dc.subject | Dengue virus | |
dc.subject | Flavivirus | |
dc.subject | Amino Acid Sequence | |
dc.subject | Binding Sites | |
dc.subject | Crystallography, X-Ray | |
dc.subject | Dengue Virus | |
dc.subject | Methyltransferases | |
dc.subject | Models, Molecular | |
dc.subject | Molecular Sequence Data | |
dc.subject | Nucleic Acid Conformation | |
dc.subject | Protein Binding | |
dc.subject | Protein Structure, Tertiary | |
dc.subject | RNA Caps | |
dc.subject | RNA, Viral | |
dc.subject | Viral Proteins | |
dc.type | Article | |
dc.contributor.department | DEAN'S OFFICE (DUKE-NUS MEDICAL SCHOOL) | |
dc.contributor.department | DUKE-NUS MEDICAL SCHOOL | |
dc.description.doi | 10.1371/journal.pone.0012836 | |
dc.description.sourcetitle | PLoS ONE | |
dc.description.volume | 5 | |
dc.description.issue | 9 | |
dc.description.page | 1-9 | |
Appears in Collections: | Elements Staff Publications |
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