› 3c3y

X-ray diffraction
1.37Å resolution

Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum

Released:
DOI: 10.2210/pdb3c3y/pdb
PDB entry 3c3y coloured by chain, front view.
PDB entry 3c3y coloured by chain, side view.
PDB entry 3c3y coloured by chain, top view.
Source organism: Mesembryanthemum crystallinum
Primary publication:
Biochemical and structural analysis of substrate promiscuity in plant Mg2+-dependent O-methyltransferases.
Kopycki JG, Rauh D, Chumanevich AA, Neumann P, Vogt T, Stubbs MT
J Mol Biol 378 154-64 (2008)
PMID: 18342334

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + feruloyl-CoA
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-180556 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 26.62 KDa
Source organism: Mesembryanthemum crystallinum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6YI95 (Residues: 1-237; Coverage: 100%)
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 48.89Å b: 71.83Å c: 128.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.222
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The rise of chemodiversity in plants.
Weng et al. (2012)
4 more

6 mentions without citation

Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.
Lashley et al. (2022)
5 more