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_39
Snippet: Overall, our data identifies a key role of residue D265 within the catalytic tetrad to maintain 2 0 -O MT function of VP4. Further, it highlights that the triple residues (N311, Y334 and R367) mutated in combination perturb the efficiency of catalytic activity of VP4 for cap1 formation at the 5 0 termini of the transcripts......
Document: Overall, our data identifies a key role of residue D265 within the catalytic tetrad to maintain 2 0 -O MT function of VP4. Further, it highlights that the triple residues (N311, Y334 and R367) mutated in combination perturb the efficiency of catalytic activity of VP4 for cap1 formation at the 5 0 termini of the transcripts.
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