› 2xrq

X-ray diffraction
2.4Å resolution

Crystal structures exploring the origins of the broader specificity of escherichia coli heat-labile enterotoxin compared to cholera toxin

Released:
DOI: 10.2210/pdb2xrq/pdb
PDB entry 2xrq coloured by chain, front view.
PDB entry 2xrq coloured by chain, side view.
PDB entry 2xrq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures exploring the origins of the broader specificity of escherichia coli heat-labile enterotoxin compared to cholera toxin.
Holmner A, Mackenzie A, Okvist M, Jansson L, Lebens M, Teneberg S, Krengel U
J Mol Biol 406 387-402 (2011)
PMID: 21168418

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Heat-labile enterotoxin B chain Chains: D, E, F, G, H
Molecule details ›
Chains: D, E, F, G, H
Length: 103 amino acids
Theoretical weight: 11.81 KDa
Source organism: Escherichia coli
Expression system: Vibrio cholerae
UniProt:
  • Canonical: P32890 (Residues: 22-124; Coverage: 100%)
Gene names: eltB, ltpB
Sequence domains: Heat-labile enterotoxin beta chain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL, NGA, SIA
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: C2
Unit cell:
a: 112.009Å b: 96.099Å c: 66.289Å
α: 90° β: 97.22° γ: 90°
R-values:
R R work R free
0.213 0.212 0.235
Expression system: Vibrio cholerae

Quick links

Citations

2 review citations

Sialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration.
Schnaar et al. (2014)
1 more

1 mention without citation

Specificity of Escherichia coli Heat-Labile Enterotoxin Investigated by Single-Site Mutagenesis and Crystallography.
Heggelund et al. (2019)