2oy0

X-ray diffraction
2.8Å resolution

Crystal structure of the West Nile virus methyltransferase

Released:
Source organism: West Nile virus
Primary publication:
Structure and function of flavivirus NS5 methyltransferase.
J Virol 81 3891-903 (2007)
PMID: 17267492

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-192974 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase NS5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 30.06 KDa
Source organism: West Nile virus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Q6P4 (Residues: 2534-2795; Coverage: 8%)
Gene names: GP1, MZ11_60484gpGP1, MZ11_60553gpGP1
Sequence domains: FtsJ-like methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P1
Unit cell:
a: 39.229Å b: 66.009Å c: 78.761Å
α: 112.46° β: 102.9° γ: 89.8°
R-values:
R R work R free
0.259 0.259 0.334
Expression system: Escherichia coli