› 5oon

X-ray diffraction
2.6Å resolution

Structure of Undecaprenyl-Pyrophosphate Phosphatase, BacA

Released:
DOI: 10.2210/pdb5oon/pdb
PDB entry 5oon coloured by chain, front view.
PDB entry 5oon coloured by chain, side view.
PDB entry 5oon coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis.
El Ghachi M, Howe N, Huang CY, Olieric V, Warshamanage R, Touzé T, Weichert D, Stansfeld PJ, Wang M, Kerff F, Caffrey M
Nat Commun 9 1078 (2018)
PMID: 29540682

Function and Biology Details

Reaction catalysed: 
Ditrans,octacis-undecaprenyl diphosphate + H(2)O = ditrans,octacis-undecaprenyl phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-199663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Undecaprenyl-diphosphatase Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 30.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli DH1
UniProt:
  • Canonical: P60932 (Residues: 1-273; Coverage: 100%)
Gene names: JW3029, b3057, bacA, upk, uppP
Sequence domains: Bacitracin resistance protein BacA

Ligands and Environments

3 bound ligands:
Ligand HG 2 x HG
Ligand TRS 1 x TRS
Ligand OLC 2 x OLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C222
Unit cell:
a: 113.26Å b: 145Å c: 40.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.244
Expression system: Escherichia coli DH1

Quick links

Citations

4 review citations

Structure and Mechanism of the Lipid Flippase MurJ.
Kuk et al. (2022)
3 more

4 mentions without citation

Structure, catalysis, and inhibition mechanism of prenyltransferase.
Chang et al. (2021)
3 more