› 2aet

X-ray diffraction
2.75Å resolution

R304K trichodiene synthase: Complex with Mg, pyrophosphate, and (4S)-7-azabisabolene

Released:
DOI: 10.2210/pdb2aet/pdb
PDB entry 2aet coloured by chain, front view.
PDB entry 2aet coloured by chain, side view.
PDB entry 2aet coloured by chain, top view.
Source organism: Fusarium sporotrichioides
Primary publication:
Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase.
Vedula LS, Cane DE, Christianson DW
Biochemistry 44 12719-27 (2005)
PMID: 16171386

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-146630 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trichodiene synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 44.02 KDa
Source organism: Fusarium sporotrichioides
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13513 (Residues: 1-374; Coverage: 100%)
Gene names: TOX 5, TRI5
Sequence domains: Trichodiene synthase (TRI5)
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

3 bound ligands:
Ligand EDO 2 x EDO
Ligand MG 3 x MG
Ligand POP 1 x POP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P3121
Unit cell:
a: 122.38Å b: 122.38Å c: 151.09Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

1 mention without citation

Role of arginine-304 in the diphosphate-triggered active site closure mechanism of trichodiene synthase.
Vedula et al. (2005)