› 3c3x

X-ray diffraction
2.15Å resolution

The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct lineages

Released:
DOI: 10.2210/pdb3c3x/pdb
PDB entry 3c3x coloured by chain, front view.
PDB entry 3c3x coloured by chain, side view.
PDB entry 3c3x coloured by chain, top view.
Source organism: Ocimum basilicum
Primary publication:
The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages.
Koeduka T, Louie GV, Orlova I, Kish CM, Ibdah M, Wilkerson CG, Bowman ME, Baiga TJ, Noel JP, Dudareva N, Pichersky E
Plant J 54 362-74 (2008)
PMID: 18208524

Function and Biology Details

Reaction catalysed: 
Eugenol + a carboxylate + NADP(+) = a coniferyl ester + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Eugenol synthase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 318 amino acids
Theoretical weight: 35.99 KDa
Source organism: Ocimum basilicum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15GI4 (Residues: 1-314; Coverage: 100%)
Gene name: EGS1
Sequence domains: NmrA-like family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NAP 2 x NAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 79.168Å b: 85.046Å c: 99.082Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.255 0.287
Expression system: Escherichia coli BL21(DE3)

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Citations

8 review citations

Biosynthesis, function and metabolic engineering of plant volatile organic compounds.
Dudareva et al. (2013)
7 more