› 1o9g

X-ray diffraction
1.5Å resolution

rRNA methyltransferase aviRa from Streptomyces viridochromogenes at 1.5A

Released:
DOI: 10.2210/pdb1o9g/pdb
PDB entry 1o9g coloured by chain, front view.
PDB entry 1o9g coloured by chain, side view.
PDB entry 1o9g coloured by chain, top view.
Source organism: Streptomyces viridochromogenes
Primary publication:
Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes.
Mosbacher TG, Bechthold A, Schulz GE
J Mol Biol 329 147-57 (2003)
PMID: 12742024

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + guanine(2535) in 23S rRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(2535) in 23S rRNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
23S rRNA (guanine(2535)-N(1))-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 250 amino acids
Theoretical weight: 26.83 KDa
Source organism: Streptomyces viridochromogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F5K5 (Residues: 1-250; Coverage: 100%)
Gene name: aviRa
Sequence domains: RRNA methyltransferase AviRa
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21
Unit cell:
a: 36.362Å b: 47.32Å c: 63.385Å
α: 90° β: 99.44° γ: 90°
R-values:
R R work R free
0.17 0.169 0.202
Expression system: Escherichia coli

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Citations

1 review citation

Bioactive oligosaccharide natural products.
McCranie et al. (2014)
5 other articles

1 mention without citation

Structures of ribonucleoprotein particle modification enzymes.
Liang et al. (2011)