› 2e9a

X-ray diffraction
2.1Å resolution

E. coli undecaprenyl pyrophosphate synthase in complex with BPH-628

Released:
DOI: 10.2210/pdb2e9a/pdb
PDB entry 2e9a coloured by chain, front view.
PDB entry 2e9a coloured by chain, side view.
PDB entry 2e9a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases.
Guo RT, Cao R, Liang PH, Ko TP, Chang TH, Hudock MP, Jeng WY, Chen CK, Zhang Y, Song Y, Kuo CJ, Yin F, Oldfield E, Wang AH
Proc Natl Acad Sci U S A 104 10022-7 (2007)
PMID: 17535895

Function and Biology Details

Reaction catalysed: 
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl 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-158013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) Chains: A, B
Molecule details ›
Chains: A, B
Length: 253 amino acids
Theoretical weight: 28.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60472 (Residues: 1-253; Coverage: 100%)
Gene names: JW0169, b0174, ispU, rth, uppS, yaeS
Sequence domains: Putative undecaprenyl diphosphate synthase
Structure domains: Decaprenyl diphosphate synthase-like

Ligands and Environments

1 bound ligand:
Ligand B28 3 x B28
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 63.682Å b: 68.157Å c: 109.886Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

28 review citations

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

3 mentions without citation

Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases.
Guo et al. (2007)
2 more