› 3bnx

X-ray diffraction
2.1Å resolution

Crystal structure of Aristolochene synthase complexed with farnesyl diphosphate

Released:
DOI: 10.2210/pdb3bnx/pdb
PDB entry 3bnx coloured by chain, front view.
PDB entry 3bnx coloured by chain, side view.
PDB entry 3bnx coloured by chain, top view.
Source organism: Aspergillus terreus
Primary publication:
X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis.
Shishova EY, Yu F, Miller DJ, Faraldos JA, Zhao Y, Coates RM, Allemann RK, Cane DE, Christianson DW
J Biol Chem 283 15431-9 (2008)
PMID: 18385128

Function and Biology Details

Reaction catalysed: 
(2E,6E)-farnesyl diphosphate = aristolochene + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-194078 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aristolochene synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 320 amino acids
Theoretical weight: 36.52 KDa
Source organism: Aspergillus terreus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UR08 (Residues: 1-320; Coverage: 100%)
Gene name: Ari1
Sequence domains: Terpene synthase family 2, C-terminal metal binding
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

5 bound ligands:
Ligand BME 5 x BME
Ligand FPP 3 x FPP
Ligand GOL 1 x GOL
Ligand MG 1 x MG
Ligand POP 1 x POP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 61.894Å b: 147.374Å c: 84.206Å
α: 90° β: 97.72° γ: 90°
R-values:
R R work R free
0.24 0.24 0.278
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

2 mentions without citation

X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis.
Shishova et al. (2008)
1 more