› 2jfo

X-ray diffraction
2.5Å resolution

Crystal structure of Enterococcus faecalis glutamate racemase in complex with D- and L-Glutamate

Released:
DOI: 10.2210/pdb2jfo/pdb
PDB entry 2jfo coloured by chain, front view.
PDB entry 2jfo coloured by chain, side view.
PDB entry 2jfo coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
Exploitation of structural and regulatory diversity in glutamate racemases.
Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL
Nature 447 817-22 (2007)
PMID: 17568739

Function and Biology Details

Reaction catalysed: 
L-glutamate = D-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182828 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate racemase Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 31.61 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q836J0 (Residues: 1-273; Coverage: 100%)
Gene names: EF_1121, murI
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand GLU 1 x GLU
Ligand DGL 1 x DGL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 60.29Å b: 82.08Å c: 111.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.257
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

1 mention without citation

Flooding enzymes: quantifying the contributions of interstitial water and cavity shape to ligand binding using extended linear response free energy calculations.
Whalen et al. (2013)