› 1fp2

X-ray diffraction
1.4Å resolution

CRYSTAL STRUCTURE ANALYSIS OF ISOFLAVONE O-METHYLTRANSFERASE

Released:
DOI: 10.2210/pdb1fp2/pdb
PDB entry 1fp2 coloured by chain, front view.
PDB entry 1fp2 coloured by chain, side view.
PDB entry 1fp2 coloured by chain, top view.
Source organism: Medicago sativa
Primary publication:
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
Zubieta C, He XZ, Dixon RA, Noel JP
Nat Struct Biol 8 271-9 (2001)
PMID: 11224575

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a 7-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 7-methoxyisoflavone
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-127675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoflavone-7-O-methyltransferase 8 Chain: A
Molecule details ›
Chain: A
Length: 352 amino acids
Theoretical weight: 39.65 KDa
Source organism: Medicago sativa
Expression system: Escherichia coli
UniProt:
  • Canonical: O24529 (Residues: 1-352; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
Ligand HMO 1 x HMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2
Unit cell:
a: 145.556Å b: 50.538Å c: 63.824Å
α: 90° β: 106.69° γ: 90°
R-values:
R R work R free
0.233 0.217 0.233
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Natural products and plant disease resistance.
Dixon RA. (2001)
24 more

13 mentions without citation

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