Author: Stewart, Meredith E.; Roy, Polly
Title: Structure-based identification of functional residues in the nucleoside-2'-O-methylase domain of Bluetongue virus VP4 capping enzyme Document date: 2015_2_24
ID: vzel6r43_56
Snippet: We have shown that structure-based rationally-designed mutations within the VP4 2 0 -O MTase domain did not affect the function of the other domains of the protein suggesting that each domain is likely to be functionally segregated. Our genetic and biochemical data demonstrates that mutations in VP4 have a deleterious effect on the kinetics of cap1 synthesis and virus replication. Thus, not only is the preservation of the catalytic tetrad importa.....
Document: We have shown that structure-based rationally-designed mutations within the VP4 2 0 -O MTase domain did not affect the function of the other domains of the protein suggesting that each domain is likely to be functionally segregated. Our genetic and biochemical data demonstrates that mutations in VP4 have a deleterious effect on the kinetics of cap1 synthesis and virus replication. Thus, not only is the preservation of the catalytic tetrad important, the positioning the cap0 structure in the catalytic domain is critical for in vitro activity. The results presented here have contributed our understanding of the role of VP4 in BTV replication and increased our knowledge in mRNA cap methylation for the members of the Reoviridae.
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