› 1tw2

X-ray diffraction
2.5Å resolution

Crystal structure of Carminomycin-4-O-methyltransferase (DnrK) in complex with S-adenosyl-L-homocystein (SAH) and 4-methoxy-e-rhodomycin T (M-ET)

Released:
DOI: 10.2210/pdb1tw2/pdb
PDB entry 1tw2 coloured by chain, front view.
PDB entry 1tw2 coloured by chain, side view.
PDB entry 1tw2 coloured by chain, top view.
Source organism: Streptomyces peucetius
Primary publication:
Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products.
Jansson A, Koskiniemi H, Mäntsälä P, Niemi J, Schneider G
J Biol Chem 279 41149-56 (2004)
PMID: 15273252

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + carminomycin = S-adenosyl-L-homocysteine + daunorubicin
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170362 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carminomycin 4-O-methyltransferase DnrK Chains: A, B
Molecule details ›
Chains: A, B
Length: 360 amino acids
Theoretical weight: 39.14 KDa
Source organism: Streptomyces peucetius
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06528 (Residues: 2-356; Coverage: 100%)
Gene name: dnrK
Sequence domains: O-methyltransferase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SAH 2 x SAH
Ligand ERT 2 x ERT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 60.682Å b: 102.582Å c: 124.256Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.271
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork.
Hertweck et al. (2007)
7 more

9 mentions without citation

Methyltransferases: Functions and Applications.
Abdelraheem et al. (2022)
8 more