› 1rqi

X-ray diffraction
2.42Å resolution

Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate

Released:
DOI: 10.2210/pdb1rqi/pdb
PDB entry 1rqi coloured by chain, front view.
PDB entry 1rqi coloured by chain, side view.
PDB entry 1rqi coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis.
Hosfield DJ, Zhang Y, Dougan DR, Broun A, Tari LW, Swanson RV, Finn J
J Biol Chem 279 8526-9 (2004)
PMID: 14672944

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl diphosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 300 amino acids
Theoretical weight: 32.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P22939 (Residues: 1-299; Coverage: 100%)
Gene names: JW0411, b0421, ispA
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

4 bound ligands:
Ligand MG 6 x MG
Ligand DST 2 x DST
Ligand IPR 2 x IPR
Ligand DPO 1 x DPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P4122
Unit cell:
a: 88.839Å b: 88.839Å c: 174.769Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.259
Expression system: Escherichia coli

Quick links

Citations

28 review citations

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

20 mentions without citation

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