› 5mgz

X-ray diffraction
1.9Å resolution

Streptomyces Spheroides NovO (8-demethylnovbiocic acid methyltransferase) with SAH

Released:
DOI: 10.2210/pdb5mgz/pdb
PDB entry 5mgz coloured by chain, front view.
PDB entry 5mgz coloured by chain, side view.
PDB entry 5mgz coloured by chain, top view.
Source organism: Streptomyces niveus
Primary publication:
Structural and Functional Basis of C-Methylation of Coumarin Scaffolds by NovO.
Sadler JC, Chung CH, Mosley JE, Burley GA, Humphreys LD
ACS Chem Biol 12 374-379 (2017)
PMID: 28068060

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + 8-demethylnovobiocic acid = S-adenosyl-L-homocysteine + novobiocic acid
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-192232 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
8-demethylnovobiocic acid C(8)-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 236 amino acids
Theoretical weight: 26.26 KDa
Source organism: Streptomyces niveus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L9F3 (Residues: 1-230; Coverage: 100%)
Gene name: novO
Sequence domains: Methyltransferase domain

Ligands and Environments

3 bound ligands:
Ligand SAH 2 x SAH
Ligand GOL 1 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 43.724Å b: 66.97Å c: 80.563Å
α: 90° β: 92.99° γ: 90°
R-values:
R R work R free
0.179 0.178 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

A Tandem Enzymatic sp2 -C-Methylation Process: Coupling in Situ S-Adenosyl-l-Methionine Formation with Methyl Transfer.
Sadler et al. (2017)
5 more

1 mention without citation

Biocatalytic Friedel-Crafts Reactions.
Leveson-Gower et al. (2022)