› 1kyw

X-ray diffraction
2.4Å resolution

Crystal Structure Analysis of Caffeic Acid/5-hydroxyferulic acid 3/5-O-methyltransferase in complex with 5-hydroxyconiferaldehyde

Released:
DOI: 10.2210/pdb1kyw/pdb
PDB entry 1kyw coloured by chain, front view.
PDB entry 1kyw coloured by chain, side view.
PDB entry 1kyw coloured by chain, top view.
Source organism: Medicago sativa
Primary publication:
Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase.
Zubieta C, Kota P, Ferrer JL, Dixon RA, Noel JP
Plant Cell 14 1265-77 (2002)
PMID: 12084826

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate
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-151144 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caffeic acid 3-O-methyltransferase Chains: A, C, F
Molecule details ›
Chains: A, C, F
Length: 365 amino acids
Theoretical weight: 39.99 KDa
Source organism: Medicago sativa
Expression system: Escherichia coli
UniProt:
  • Canonical: P28002 (Residues: 1-365; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P2
Unit cell:
a: 104.473Å b: 61.996Å c: 112.213Å
α: 90° β: 111.27° γ: 90°
R-values:
R R work R free
0.207 0.207 0.261
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Lignin biosynthesis.
Boerjan et al. (2003)
8 more

9 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
8 more