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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
protein DENV 3
unclassified drug
virus RNA
capped RNA
virus protein
virus RNA
5' untranslated region
base pairing
crystal structure
Dengue virus
enzyme defect
enzyme structure
protein methylation
protein RNA binding
RNA stability
RNA structure
structure analysis
virus genome
amino acid sequence
binding site
chemical structure
molecular genetics
protein binding
protein tertiary structure
X ray crystallography
Dengue virus
Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
Dengue Virus
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.
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
ISSN: 19326203
DOI: 10.1371/journal.pone.0012836
Rights: Attribution 4.0 International
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