› 1dlg

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE C115S ENTEROBACTER CLOACAE MURA IN THE UN-LIGANDED STATE

Released:
DOI: 10.2210/pdb1dlg/pdb
PDB entry 1dlg coloured by chain, front view.
PDB entry 1dlg coloured by chain, side view.
PDB entry 1dlg coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA.
Schönbrunn E, Eschenburg S, Krekel F, Luger K, Amrhein N
Biochemistry 39 2164-73 (2000)
PMID: 10694381

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
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: 44.81 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 9 x PO4
Ligand HAI 3 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: 86.685Å b: 155.532Å c: 83.82Å
α: 90° β: 91.82° γ: 90°
R-values:
R R work R free
0.173 0.173 0.197
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

2 mentions without citation

The nonconserved wrapping of conserved protein folds reveals a trend toward increasing connectivity in proteomic networks.
Fernández et al. (2004)
1 more