Wesselsbron virus Methyltransferase in complex with AdoMet and 7MeGpppG

Recognition of RNA Cap in the Wesselsbron Virus NS5 Methyltransferase Domain: Implications for RNA-Capping Mechanisms in Flavivirus

NS5 N-terminal methyltransferase domain, UNP residues 2500-2791

MKHHHHHHGKAAGVTLGEVWKRQLNMLGKQEFERYKVSDITEVDRTAARRYLKEGRTDVGISVSRGAAKIRWLHERGYLR
ITGRVLDLGCGRGGWSYYAAAQKEVMSVKGYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSDTLLCDIGESSS
NPLVERDRTMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLRFGGGIVRVPFSRNSTHEMYYISGARNNITHM
VNTTSRSLLRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKT

10mM AdoMet, 1mM 7MeGpppG, 18% PEG 4000, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

The same protein in complex with Sinefungin

The same protein complexed with AdoMet and GpppG

The same protein complexed with Sinefungin and 7MeGpppA

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Flavivirus, RNA capping, Methyltransferase, Guanylyltransferase, viral enzyme structure, TRANSFERASE

GKAAGVTLGEVWKRQLNMLGKQEFERYKVSDITEVDRTAARRYLKEGRTDVGISVSRGAAKIRWLHERGYLRITGRVLDL
GCGRGGWSYYAAAQKEVMSVKGYTLGIEGHEKPIHMQTLGWNIVKFKDKSNVFTMPTEPSDTLLCDIGESSSNPLVERDR
TMKVLENFERWKHVNTENFCVKVLAPYHPDVIEKLERLQLRFGGGIVRVPFSRNSTHEMYYISGARNNITHMVNTTSRSL
LRRMTRPSGKAIIEGDVFLPTGTRSVASEAGTIDHEALKLRVDQIKAEYSKT