› 1jsz

X-ray diffraction
1.93Å resolution

Crystal Structure Analysis of N7,9-dimethylguanine-VP39 complex

Released:
DOI: 10.2210/pdb1jsz/pdb
PDB entry 1jsz coloured by chain, front view.
PDB entry 1jsz coloured by chain, side view.
PDB entry 1jsz coloured by chain, top view.
Source organism: Vaccinia virus
Primary publication:
The "cap-binding slot" of an mRNA cap-binding protein: quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap.
Hu G, Oguro A, Li C, Gershon PD, Quiocho FA
Biochemistry 41 7677-87 (2002)
PMID: 12056899

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139665 (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
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 NDM 1 x NDM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 84.3Å b: 67.7Å c: 79.6Å
α: 90° β: 118.1° γ: 90°
R-values:
R R work R free
0.224 0.21 0.252
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cap and cap-binding proteins in the control of gene expression.
Topisirovic et al. (2011)
1 more

3 mentions without citation

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