› 3i4z

X-ray diffraction
1.76Å resolution

Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus

Released:
DOI: 10.2210/pdb3i4z/pdb
PDB entry 3i4z coloured by chain, front view.
PDB entry 3i4z coloured by chain, side view.
PDB entry 3i4z coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.
Metzger U, Schall C, Zocher G, Unsöld I, Stec E, Li SM, Heide L, Stehle T
Proc Natl Acad Sci U S A 106 14309-14 (2009)
PMID: 19706516

Function and Biology Details

Reaction catalysed: 
Dimethylallyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan
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-175897 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan dimethylallyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 465 amino acids
Theoretical weight: 52.99 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q50EL0 (Residues: 1-459; Coverage: 100%)
Gene names: AFUA_2G18040, dmaW, fgaPT2
Sequence domains: Tryptophan dimethylallyltransferase

Ligands and Environments

2 bound ligands:
Ligand BU2 8 x BU2
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4, RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 80.06Å b: 98.79Å c: 125.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.151 0.183
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Structural and Chemical Biology of Terpenoid Cyclases.
Christianson DW. (2017)
26 more

4 mentions without citation

The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.
Metzger et al. (2009)
3 more