› 3cqj

X-ray diffraction
2.04Å resolution

Crystal Structure of L-xylulose-5-phosphate 3-epimerase UlaE (form B) complex with Zn2+

Released:
DOI: 10.2210/pdb3cqj/pdb
PDB entry 3cqj coloured by chain, front view.
PDB entry 3cqj coloured by chain, side view.
PDB entry 3cqj 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: 33.29 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 ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2221
Unit cell:
a: 104.208Å b: 132.596Å c: 81.798Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.213
Expression system: Escherichia coli

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Citations

2 review citations

Engineering microbial pathways for production of bio-based chemicals from lignocellulosic sugars: current status and perspectives.
Francois et al. (2020)
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