› 3p9i

X-ray diffraction
1.85Å resolution

Crystal structure of perennial ryegrass LpOMT1 complexed with S-adenosyl-L-homocysteine and sinapaldehyde

Released:
DOI: 10.2210/pdb3p9i/pdb
PDB entry 3p9i coloured by chain, front view.
PDB entry 3p9i coloured by chain, side view.
PDB entry 3p9i coloured by chain, top view.
Source organism: Lolium perenne
Primary publication:
Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference.
Louie GV, Bowman ME, Tu Y, Mouradov A, Spangenberg G, Noel JP
Plant Cell 22 4114-27 (2010)
PMID: 21177481

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
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-195710 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caffeic acid O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 364 amino acids
Theoretical weight: 39.15 KDa
Source organism: Lolium perenne
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ZTU2 (Residues: 1-360; Coverage: 100%)
Gene name: OMT1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
2 bound ligands:
Ligand SNY 4 x SNY
Ligand BME 8 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 94.938Å b: 85.225Å c: 98.568Å
α: 90° β: 111.1° γ: 90°
R-values:
R R work R free
0.232 0.232 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

3 mentions without citation

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