X-ray diffraction
2.05Å resolution

X-ray structure of RlmN from Escherichia coli in complex with S-adenosylmethionine


Function and Biology Details

Reaction catalysed:
2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Dual-specificity RNA methyltransferase RlmN Chains: A, B
Molecule details ›
Chains: A, B
Length: 404 amino acids
Theoretical weight: 45.33 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P36979 (Residues: 1-384; Coverage: 100%)
Gene names: JW2501, b2517, rlmN, yfgB
Sequence domains: Radical SAM superfamily
Structure domains:

Ligands and Environments

Cofactor: Ligand SAM 2 x SAM
1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 55.18Å b: 55.621Å c: 252.179Å
α: 90° β: 90° γ: 90°
R R work R free
0.204 0.202 0.242
Expression system: Escherichia coli