› 2e4o

X-ray diffraction
2.2Å resolution

X-ray Crystal Structure of Aristolochene Synthase from Aspergillus terreus and the Evolution of Templates for the Cyclization of Farnesyl Diphosphate

Released:
DOI: 10.2210/pdb2e4o/pdb
PDB entry 2e4o coloured by chain, front view.
PDB entry 2e4o coloured by chain, side view.
PDB entry 2e4o coloured by chain, top view.
Source organism: Aspergillus terreus
Primary publication:
X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate.
Shishova EY, Di Costanzo L, Cane DE, Christianson DW
Biochemistry 46 1941-51 (2007)
PMID: 17261032

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
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

3 bound ligands:
Ligand BME 5 x BME
Ligand CL 2 x CL
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 61.19Å b: 147.242Å c: 83.736Å
α: 90° β: 97.91° γ: 90°
R-values:
R R work R free
0.222 0.222 0.272
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
16 more

4 mentions without citation

Terpenoid synthase structures: a so far incomplete view of complex catalysis.
Gao et al. (2012)
3 more