› 5eat

X-ray diffraction
2.8Å resolution

5-EPI-ARISTOLOCHENE SYNTHASE FROM NICOTIANA TABACUM WITH SUBSTRATE ANALOG FARNESYL HYDROXYPHOSPHONATE

Released:
DOI: 10.2210/pdb5eat/pdb
PDB entry 5eat coloured by chain, front view.
PDB entry 5eat coloured by chain, side view.
PDB entry 5eat coloured by chain, top view.
Source organism: Nicotiana tabacum
Primary publication:
Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase.
Starks CM, Back K, Chappell J, Noel JP
Science 277 1815-20 (1997)
PMID: 9295271

Function and Biology Details

Reaction catalysed: 
(2E,6E)-farnesyl diphosphate = (+)-5-epiaristolochene + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-epi-aristolochene synthase Chain: A
Molecule details ›
Chain: A
Length: 548 amino acids
Theoretical weight: 63.07 KDa
Source organism: Nicotiana tabacum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q40577 (Residues: 1-548; Coverage: 100%)
Gene names: EAS3, EAS4
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P41212
Unit cell:
a: 126.33Å b: 126.33Å c: 121.698Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.28
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

65 review citations

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

24 mentions without citation

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