3evg

X-ray diffraction
2.2Å resolution

Crystal structure of Dengue-2 virus methyltransferase complexed with S-adenosyl-L-homocysteine

Released:
Source organism: Dengue virus 2 16681-PDK53
Primary publication:
Analysis of flavivirus NS5 methyltransferase cap binding.
J. Mol. Biol. 385 1643-54 (2009)
PMID: 19101564

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA]
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase NS5 Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 30.84 KDa
Source organism: Dengue virus 2 16681-PDK53
Expression system: Escherichia coli
UniProt:
  • Canonical: P29991 (Residues: 2493-2757; Coverage: 8%)
Sequence domains: FtsJ-like methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 112.615Å b: 112.615Å c: 55.696Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.24 0.253
Expression system: Escherichia coli