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- W2313315052 abstract "In the context of the European VIZIER project, our lab is involved in the study of flaviviral methyltransferases (MTase) and helicases (Hel). Flaviviruses are enveloped positive-strand RNA viruses, which code for 3 structural and 7 non-structural (NS) proteins. Among the NS, particularly important are the multifunctional proteins NS3 (protease/helicase) and NS5 (Mtase/RNA-polymerase). Flaviviral Hel participate in RNA replication separating the RNA template and daughter strands. We report here the three-dimensional structure (at 3.1 A resolution) of the NS3 helicase domain (residues 186-619; NS3:186-619) from Kunjin virus, an Australian variant of the West Nile virus. As for homologous helicases, NS3:186-619 is composed of three domains, two of which are structurally related and held to host the NTPase and RTPase active sites. The third domain (C-terminal) is involved in RNA binding/recognition. In addition, we analyzed the activity of the full-length protein and its structure in solution using small angle X-ray scattering (SAXS). Our results show a strong influence of the NS3 protease domain on the helicase activity that can scarcely be explained in term of domains organization and requires further investigations. MTases are involved in the mRNA capping process, resulting in the transfer of methyl groups from the cofactor S-adenosyl-L-methionine (AdoMet) to a capped RNA substrate. We solved the crystal structures of the Wesselsbron virus methyltransferase (MTase) in complex with AdoMet and with both the cofactor and the capped substrate GpppG, at 2.0 A and 1.9 A resolution, respectively. Wesselsbron is an African mosquito-borne Flavivirus belonging to the Yellow Fever virus group that affects animals and human beings. Comparison of the two structures shows that the presence of GpppG stabilizes the N-terminal subdomain, as indicated by the higher B-factor values relative to the other MTases. In order to further characterize the function and catalytic activity of MTase, assays with different substrates are in progress." @default.
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- W2313315052 date "2007-08-22" @default.
- W2313315052 modified "2023-09-27" @default.
- W2313315052 title "MTases and helicases: a medium-throughput approach to viral protein structures" @default.
- W2313315052 doi "https://doi.org/10.1107/s0108767307099424" @default.
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