Researchers decipher the structure of protein methyltransferase from the mpox virus IOCBPrague NatureComms
. Final Ramachandran statistics were as follows: favored in the range 98−100%, allowed in the range 0−2%, outliers 0%. Structural figures were generated with the PyMOL Molecular Graphics System v2.0 .For the 2′-O-MTase, an m7GpppG-capped RNA or an m7GpppA-capped RNA were used. These RNAs were 35 nucleotides long and they were prepared by in vitro transcription using a double-stranded DNA template and the TranscriptAid T7 high-yield transcription kit .
For measurements of inhibition of the 2´-O-MTase reaction the protocol was modified for 1536-well plates. The total volume was 4 µl per well and the reaction mixture contained 4 μM SAM and 4 μM m7GpppG-capped RNA in the MTase buffer. RNase inhibitor was added to the reaction in the concentration of 1 U/μl to prevent potential RNase degradation. The reaction was initiated by adding 200 nM VP39, mixed, spun, and incubated at 30 °C for 45 min.
For measurements of inhibition of the SARS-CoV-2 2′-O-MTase nsp16, a similar protocol was used. The 2´-O-MTase reaction mixture contained 500 nM SARS-CoV-2 nsp16, 8 μM SARS-CoV-2 nsp10 , 4 μM SAM, 4 μM m7GpppA-capped RNA and 1 U/μl of RNase inhibitor in the reaction buffer (5 mM Tris pH 8, 1 mM MgCl
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