› 1vpt

X-ray diffraction
1.8Å resolution

AS11 VARIANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE

Released:
DOI: 10.2210/pdb1vpt/pdb
PDB entry 1vpt coloured by chain, front view.
PDB entry 1vpt coloured by chain, side view.
PDB entry 1vpt coloured by chain, top view.
Source organism: Vaccinia virus WR
Primary publication:
The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends.
Hodel AE, Gershon PD, Shi X, Quiocho FA
Cell 85 247-56 (1996)
PMID: 8612277

Function and Biology Details

Reaction catalysed: 
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]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 348 amino acids
Theoretical weight: 39.93 KDa
Source organism: Vaccinia virus WR
Expression system: Escherichia coli
UniProt:
  • Canonical: P07617 (Residues: 1-333; Coverage: 100%)
Gene names: J3R, OPG102, PAPS, VACWR095
Sequence domains: Poly A polymerase regulatory subunit
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 85.3Å b: 67.8Å c: 80.4Å
α: 90° β: 118.4° γ: 90°
R-values:
R R work R free
0.215 0.215 0.25
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Viral and cellular mRNA capping: past and prospects.
Furuichi et al. (2000)
19 more

7 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
6 more