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› 3i4x

X-ray diffraction
2.1Å resolution

Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus in complex with Trp and DMSPP

Released:
DOI: 10.2210/pdb3i4x/pdb
Model geometry
Fit model/data
PDB entry 3i4x coloured by chain, front view.
PDB entry 3i4x coloured by chain, side view.
PDB entry 3i4x 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: 
L-tryptophan + dimethylallyl diphosphate = 4-(3-methylbut-2-enyl)-L-tryptophan + diphosphate.
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

3 bound ligands:
Ligand DST 2 x DST
Ligand TRP 2 x TRP
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 79.07Å b: 97.85Å c: 125.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.2
Expression system: Escherichia coli

Quick links

Citations

26 review citations

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

16 mentions without citation

Structure, catalysis, and inhibition mechanism of prenyltransferase.
Chang et al. (2021)
15 more