› 1ejd

X-ray diffraction
1.55Å resolution

Crystal structure of unliganded mura (type1)

Released:
DOI: 10.2210/pdb1ejd/pdb
PDB entry 1ejd coloured by chain, front view.
PDB entry 1ejd coloured by chain, side view.
PDB entry 1ejd coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
Comparative X-ray analysis of the un-liganded fosfomycin-target murA.
Eschenburg S, Schönbrunn E
Proteins 40 290-8 (2000)
PMID: 10842342

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-152534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 419 amino acids
Theoretical weight: 44.83 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli
UniProt:
  • Canonical: P33038 (Residues: 1-419; Coverage: 100%)
Gene names: ECL_04571, murA, murZ
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

2 bound ligands:
Ligand PO4 15 x PO4
Ligand HAI 5 x HAI
1 modified residue:
Ligand IAS 2 x IAS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: C2
Unit cell:
a: 87.177Å b: 156.297Å c: 84.036Å
α: 90° β: 91.63° γ: 90°
R-values:
R R work R free
0.185 0.185 0.207
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
6 more

9 mentions without citation

Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).
Zhu et al. (2012)
8 more