› 2jfn

X-ray diffraction
1.9Å resolution

Crystal structure of Escherichia coli glutamate racemase in complex with L- Glutamate and activator UDP-MurNAc-ala

Released:
DOI: 10.2210/pdb2jfn/pdb
PDB 2jfn coloured by chain and viewed from the front.
PDB 2jfn coloured by chain and viewed from the side.
PDB 2jfn coloured by chain and viewed from the top.
Source organism: Escherichia coli
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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate racemase Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 31.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P22634 (Residues: 1-285; Coverage: 100%)
Gene names: JW5550, b3967, dga, glr, murI, yijA
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 83.05Å b: 112.82Å c: 74.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.244
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.
Lloyd et al. (2021)
8 more

7 mentions without citation

Intrinsic dynamics is evolutionarily optimized to enable allosteric behavior.
Zhang et al. (2020)
6 more