› 3i5u

X-ray diffraction
2.6Å resolution

Crystal structure of an O-methyltransferase (NcsB1) from neocarzinostatin biosynthesis in complex with S-adenosylmethionine (SAM) and 2-hydroxy-5-methyl naphthoic acid (MNA)

Released:
DOI: 10.2210/pdb3i5u/pdb
PDB entry 3i5u coloured by chain, front view.
PDB entry 3i5u coloured by chain, side view.
PDB entry 3i5u coloured by chain, top view.
Source organism: Streptomyces carzinostaticus subsp. neocarzinostaticus
Primary publication:
Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
Cooke HA, Guenther EL, Luo Y, Shen B, Bruner SD
Biochemistry 48 9590-8 (2009)
PMID: 19702337

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate
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-183044 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 34.63 KDa
Source organism: Streptomyces carzinostaticus subsp. neocarzinostaticus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q84HC8 (Residues: 1-332; Coverage: 100%)
Gene name: ncsB1
Sequence domains: O-methyltransferase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SAM 2 x SAM
Ligand 5NA 2 x 5NA
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P65
Unit cell:
a: 109.083Å b: 109.083Å c: 206.884Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.206 0.227
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
1 more

2 mentions without citation

Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
Cooke et al. (2009)
1 more