ArticleProtein science : a publication of the Protein Society2007
Structural bases for substrate recognition and activity in Meaban virus nucleoside-2'-O-methyltransferase.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 40 citations in OpenAlex.
- Development in the Inhibition of Dengue Proteases as Drug Targets.Current medicinal chemistry · 2024Review
- Structural and functional basis of low-affinity SAM/SAH-binding in the conserved MTase of the multi-segmented Alongshan virus distantly related to canonical unsegmented flaviviruses.PLoS pathogens · 2023Article
- Article
- A second type of N7-guanine RNA cap methyltransferase in an unusual locus of a large RNA virus genome.Nucleic acids research · 2022Article
- Crystal Structures of Flavivirus NS5 Guanylyltransferase Reveal a GMP-Arginine Adduct.Journal of virology · 2022Article
- Crystal structure of a tick-borne flavivirus RNA-dependent RNA polymerase suggests a host adaptation hotspot in RNA viruses.Nucleic acids research · 2021Article
- The crystal structure of Zika virus NS5 reveals conserved drug targets.The EMBO journal · 2017Article
- Identification and Characterization of a Ribose 2'-O-Methyltransferase Encoded by the Ronivirus Branch of Nidovirales.Journal of virology · 2016Article
- Perturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation.Journal of virology · 2015Article
- Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase.Protein science : a publication of the Protein Society · 2015Article
- Crystal structure of dengue virus methyltransferase without S-adenosyl-L-methionine.Antiviral research · 2014Article
- Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation.Nature communications · 2014Article
- RNA methyltransferases involved in 5' cap biosynthesis.RNA biology · 2014Review
- Crystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface.PLoS pathogens · 2013Article
- Identification of a novel antiviral inhibitor of the flavivirus guanylyltransferase enzyme.Journal of virology · 2012Article
- Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase.The Journal of biological chemistry · 2010Article
- Structure and functionality in flavivirus NS-proteins: perspectives for drug design.Antiviral research · 2010Review
- Flavivirus RNA cap methyltransferase: structure, function, and inhibition.Frontiers in biology · 2010Article
- Flaviviral methyltransferase/RNA interaction: structural basis for enzyme inhibition.Antiviral research · 2009Article
- Analysis of flavivirus NS5 methyltransferase cap binding.Journal of molecular biology · 2009Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viral methyltransferases are involved in the mRNA capping process, resulting in the transfer of a methyl group from S-adenosyl-L-methionine to capped RNA. Two groups of methyltransferases (MTases) are known: (guanine-N7)-methyltransferases (N7MTases), adding a methyl group onto the N7 atom of guanine, and (nucleoside-2'-O-)-methyltransferases (2'OMTases), adding a methyl group to a ribose hydroxyl. We have expressed and purified two constructs of Meaban virus (MV; genus Flavivirus) NS5 protein MTase domain (residues 1-265 and 1-293, respectively). We report here the three-dimensional structure of the shorter MTase construct in complex with the cofactor S-adenosyl-L-methionine, at 2.9 angstroms resolution. Inspection of the refined crystal structure, which highlights structural conservation of specific active site residues, together with sequence analysis and structural comparison with Dengue virus 2'OMTase, suggests that the crystallized enzyme belongs to the 2'OMTase subgroup. Enzymatic assays show that the short MV MTase construct is inactive, but the longer construct expressed can transfer a methyl group to the ribose 2'O atom of a short GpppAC(5) substrate. West Nile virus MTase domain has been recently shown to display both N7 and 2'O MTase activity on a capped RNA substrate comprising the 5'-terminal 190 nt of the West Nile virus genome. The lack of N7 MTase activity here reported for MV MTase may be related either to the small size of the capped RNA substrate, to its sequence, or to different structural properties of the C-terminal regions of West Nile virus and MV MTase-domains.
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