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_50
Snippet: BTV VP4, unlike many other viral capping enzymes, possesses all the catalytic activities required for the generation of methylated cap structure at the 5 0 terminus of BTV transcripts. Crystal structure of VP4 revealed that the protein consisted of four independent, discrete functional domains each with a discrete role in the capping pathway. The putative 2 0 -O MTase domain which is were detected using monospecific polyclonal antibodies; aVP3 or.....
Document: BTV VP4, unlike many other viral capping enzymes, possesses all the catalytic activities required for the generation of methylated cap structure at the 5 0 terminus of BTV transcripts. Crystal structure of VP4 revealed that the protein consisted of four independent, discrete functional domains each with a discrete role in the capping pathway. The putative 2 0 -O MTase domain which is were detected using monospecific polyclonal antibodies; aVP3 or aNS1 respectively. As a loading control, cellular protein b-actin was detected using aActin antibody responsible for the last catalytic reaction of the cap structure, is attached via a small linker to the other upstream enzymatic domains including kinase-like, GT and N7-MT that are responsible for the upstream reactions of pathway. The highly ordered structure of VP4 highlighted the importance of synthesizing BTV cap in a sequential manner. To date no functions have been assigned to any domain of VP4 and the purpose of this report was to obtain structure-based biochemical evidence for function focussing mainly on the 2 0 -O MTase domain by generating a series of targeted mutations in the recombinant VP4 as well as in the replicating viral genome.
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