› 3mag

X-ray diffraction
1.8Å resolution

VACCINIA METHYLTRANSFERASE VP39 COMPLEXED WITH M3ADE AND S-ADENOSYLHOMOCYSTEINE

Released:
DOI: 10.2210/pdb3mag/pdb
PDB entry 3mag coloured by chain, front view.
PDB entry 3mag coloured by chain, side view.
PDB entry 3mag coloured by chain, top view.
Source organism: Vaccinia virus
Primary publication:
mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains.
Hu G, Gershon PD, Hodel AE, Quiocho FA
Proc Natl Acad Sci U S A 96 7149-54 (1999)
PMID: 10377383

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: 307 amino acids
Theoretical weight: 35.92 KDa
Source organism: Vaccinia virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07617 (Residues: 1-307; Coverage: 92%)
Gene names: J3R, OPG102, PAPS, VACWR095
Sequence domains: Poly A polymerase regulatory subunit
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
Ligand 3MA 1 x 3MA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 84.5Å b: 67.21Å c: 79.56Å
α: 90° β: 117.3° γ: 90°
R-values:
R R work R free
0.217 0.217 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

6 mentions without citation

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