› 1eyn

X-ray diffraction
1.7Å resolution

Structure of mura liganded with the extrinsic fluorescence probe ANS

Released:
DOI: 10.2210/pdb1eyn/pdb
PDB entry 1eyn coloured by chain, front view.
PDB entry 1eyn coloured by chain, side view.
PDB entry 1eyn coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA.
Schonbrunn E, Eschenburg S, Luger K, Kabsch W, Amrhein N
Proc Natl Acad Sci U S A 97 6345-9 (2000)
PMID: 10823915

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chain: A
Molecule details ›
Chain: A
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 2AN 1 x 2AN
Ligand GOL 2 x GOL
1 modified residue:
Ligand IAS 1 x IAS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 62.1Å b: 66.6Å c: 107.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.21
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

3 mentions without citation

ANS fluorescence: potential to augment the identification of the external binding sites of proteins.
Gasymov et al. (2007)
2 more