› 1ri4

X-ray diffraction
2.4Å resolution

Structure and mechanism of mRNA cap (guanine N-7) methyltransferase

Released:
DOI: 10.2210/pdb1ri4/pdb
PDB entry 1ri4 coloured by chain, front view.
PDB entry 1ri4 coloured by chain, side view.
PDB entry 1ri4 coloured by chain, top view.
Source organism: Encephalitozoon cuniculi
Primary publication:
Structure and mechanism of mRNA cap (guanine-N7) methyltransferase.
Fabrega C, Hausmann S, Shen V, Shuman S, Lima CD
Mol Cell 13 77-89 (2004)
PMID: 14731396

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[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-186086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
mRNA cap guanine-N(7) methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 34.82 KDa
Source organism: Encephalitozoon cuniculi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8SR66 (Residues: 1-283; Coverage: 100%)
Gene names: ABD1, ECU10_0380
Sequence domains: mRNA (guanine-N(7))-methyltransferase domain
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
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 63.803Å b: 63.803Å c: 112.683Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.271
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

21 review citations

mRNA capping: biological functions and applications.
Ramanathan et al. (2016)
20 more

6 mentions without citation

RNA methyltransferases involved in 5' cap biosynthesis.
Byszewska et al. (2014)
5 more