› 3fzg

X-ray diffraction
2Å resolution

Structure of the 16S rRNA methylase ArmA

Released:
DOI: 10.2210/pdb3fzg/pdb
PDB entry 3fzg coloured by chain, front view.
PDB entry 3fzg coloured by chain, side view.
PDB entry 3fzg coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases.
Schmitt E, Galimand M, Panvert M, Courvalin P, Mechulam Y
J Mol Biol 388 570-82 (2009)
PMID: 19303884

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + guanine(1405) in 16S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(1405) in 16S rRNA
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
16S rRNA (guanine(1405)-N(7))-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 23.38 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6F5A0 (Residues: 58-257; Coverage: 78%)
Gene names: BGZ_00007, BGZ_00015, BGZ_00045, BGZ_05224, BGZ_05455, HLZ50_23845, HLZ50_26645, RCS40_P0051, armA, pMUR050_016
Sequence domains: Ribosomal RNA methyltransferase (FmrO)
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: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 74.11Å b: 90.08Å c: 65.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.206
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Ribosome-targeting antibiotics and resistance via ribosomal RNA methylation.
Jeremia et al. (2023)
20 other articles

3 mentions without citation

Mechanisms of Resistance to Aminoglycoside Antibiotics: Overview and Perspectives.
Garneau-Tsodikova et al. (2016)
2 more