› 3gyq

X-ray diffraction
2.45Å resolution

Structure of the Thiostrepton-Resistance Methyltransferase S-adenosyl-L-methionine Complex

Released:
DOI: 10.2210/pdb3gyq/pdb
PDB entry 3gyq coloured by chain, front view.
PDB entry 3gyq coloured by chain, side view.
PDB entry 3gyq coloured by chain, top view.
Source organism: Streptomyces cyaneus
Primary publication:
Structure of the thiostrepton resistance methyltransferase.S-adenosyl-L-methionine complex and its interaction with ribosomal RNA.
Dunstan MS, Hang PC, Zelinskaya NV, Honek JF, Conn GL
J Biol Chem 284 17013-17020 (2009)
PMID: 19369248

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + adenosine(1067) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyladenosine(1067) in 23S rRNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148419 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
23S rRNA (adenosine(1067)-2'-O)-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 272 amino acids
Theoretical weight: 29.22 KDa
Source organism: Streptomyces cyaneus
Expression system: Escherichia coli
UniProt:
  • Canonical: P18644 (Residues: 1-269; Coverage: 100%)
Gene names: tsnR, tsr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAM 2 x SAM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 40.96Å b: 55.77Å c: 215.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.268
Expression system: Escherichia coli

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Citations

3 review citations

Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical enzyme for bacterial metabolism.
Parveen et al. (2011)
2 more

4 mentions without citation

Tied up in knots: Untangling substrate recognition by the SPOUT methyltransferases.
Strassler et al. (2022)
3 more