› 4dcm

X-ray diffraction
2.3Å resolution

Crystal Structure of methyltransferase RlmG modifying G1835 of 23S rRNA in Escherichia coli

Released:
DOI: 10.2210/pdb4dcm/pdb
PDB entry 4dcm coloured by chain, front view.
PDB entry 4dcm coloured by chain, side view.
PDB entry 4dcm coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural insights into the function of 23S rRNA methyltransferase RlmG (m²G1835) from Escherichia coli.
Zhang H, Gao ZQ, Wei Y, Wang WJ, Liu GF, Shtykova EV, Xu JH, Dong YH
RNA 18 1500-9 (2012)
PMID: 22753782

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + guanine(1835) in 23S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(1835) in 23S rRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154833 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal RNA large subunit methyltransferase G Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 42.46 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P42596 (Residues: 9-373; Coverage: 97%)
Gene names: JW5513, b3084, rlmG, ygjO
Sequence domains: Methyltransferase small domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
1 bound ligand:
Ligand PEG 2 x PEG
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P21
Unit cell:
a: 67.185Å b: 42.134Å c: 72.429Å
α: 90° β: 104.46° γ: 90°
R-values:
R R work R free
0.203 0.201 0.252
Expression system: Escherichia coli

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Citations

4 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
3 more