› 3cqh

X-ray diffraction
2.08Å resolution

Crystal Structure of L-xylulose-5-phosphate 3-epimerase UlaE from the Anaerobic L-ascorbate Utilization Pathway of Escherichia coli

Released:
DOI: 10.2210/pdb3cqh/pdb
PDB entry 3cqh coloured by chain, front view.
PDB entry 3cqh coloured by chain, side view.
PDB entry 3cqh coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
Shi R, Pineda M, Ajamian E, Cui Q, Matte A, Cygler M
J Bacteriol 190 8137-44 (2008)
PMID: 18849419

Function and Biology Details

Reaction catalysed: 
L-ribulose 5-phosphate = L-xylulose 5-phosphate
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-186884 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ribulose-5-phosphate 3-epimerase UlaE Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 33.85 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8XDI5 (Residues: 2-284; Coverage: 100%)
Gene names: ECs5173, Z5806, ulaE
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P43212
Unit cell:
a: 110.386Å b: 110.386Å c: 103.015Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.242
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Features and applications of microbial sugar epimerases.
Ito S. (2009)
1 more

2 mentions without citation

Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
Shi et al. (2008)
1 more