4h0n

X-ray diffraction
2.71Å resolution

Crystal structure of Spodoptera frugiperda DNMT2 E260A/E261A/K263A mutant

Released:
Source organism: Spodoptera frugiperda
Primary publication:
Functional and structural characterization of DNMT2 from Spodoptera frugiperda.
J Mol Cell Biol 5 64-6 (2013)
PMID: 23103599

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + cytosine(38) in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(38) in tRNA
S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-104221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA (cytosine(38)-C(5))-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 333 amino acids
Theoretical weight: 38.45 KDa
Source organism: Spodoptera frugiperda
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2H1VE33 (Residues: 1-332; Coverage: 100%)
Gene names: DNMT2, SFRICE_001256, TRDMT1
Sequence domains: C-5 cytosine-specific DNA methylase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 97.394Å b: 106.154Å c: 151.016Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.256
Expression system: Escherichia coli BL21(DE3)