› 1zga

X-ray diffraction
2.35Å resolution

Crystal structure of isoflavanone 4'-O-methyltransferase complexed with (+)-6a-hydroxymaackiain

Released:
DOI: 10.2210/pdb1zga/pdb
PDB entry 1zga coloured by chain, front view.
PDB entry 1zga coloured by chain, side view.
PDB entry 1zga coloured by chain, top view.
Source organism: Medicago truncatula
Primary publication:
Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
Liu CJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP
Plant Cell 18 3656-69 (2006)
PMID: 17172354

Function and Biology Details

Reactions catalysed: 
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone = S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
S-adenosyl-L-methionine + a 4'-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 4'-methoxyisoflavone
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-173367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoflavone 4'-O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 40.1 KDa
Source organism: Medicago truncatula
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q29U70 (Residues: 8-364; Coverage: 98%)
Gene name: HI4'OMT
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P4322
Unit cell:
a: 71.217Å b: 71.217Å c: 188.907Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.209 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

12 review citations

Phenylpropanoid biosynthesis.
Vogt T. (2010)
11 more

2 mentions without citation

Structure and function of enzymes involved in the biosynthesis of phenylpropanoids.
Ferrer et al. (2008)
1 more