› 1fpq

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE ANALYSIS OF SELENOMETHIONINE SUBSTITUTED CHALCONE O-METHYLTRANSFERASE

Released:
DOI: 10.2210/pdb1fpq/pdb
PDB entry 1fpq coloured by chain, front view.
PDB entry 1fpq coloured by chain, side view.
PDB entry 1fpq 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

Reactions catalysed: 
S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine + 2'-O-methyllicodione
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-161075 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoliquiritigenin 2'-O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 41.88 KDa
Source organism: Medicago sativa
Expression system: Escherichia coli
UniProt:
  • Canonical: P93324 (Residues: 1-372; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
No bound ligands
1 modified residue:
Ligand MSE 15 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2
Unit cell:
a: 125.52Å b: 53.47Å c: 73.6Å
α: 90° β: 124.62° γ: 90°
R-values:
R R work R free
0.295 0.247 0.295
Expression system: Escherichia coli

Quick links

Citations

27 review citations

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

4 mentions without citation

AdoMet-dependent methylation, DNA methyltransferases and base flipping.
Cheng et al. (2001)
3 more