› 2xrs

X-ray diffraction
1.81Å resolution

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

Released:
DOI: 10.2210/pdb2xrs/pdb
PDB entry 2xrs coloured by chain, front view.
PDB entry 2xrs coloured by chain, side view.
PDB entry 2xrs 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 (3 distinct):
Heat-labile enterotoxin B chain Chains: D, E, F, G, H, L, M, N, O, P
Molecule details ›
Chains: D, E, F, G, H, L, M, N, O, P
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: GAL, NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GAL, NAG
Carbohydrate polymer
1 bound ligand:
Ligand GAL 1 x GAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P1
Unit cell:
a: 53.42Å b: 61.06Å c: 100.83Å
α: 94.57° β: 95.24° γ: 114.1°
R-values:
R R work R free
0.196 0.195 0.219
Expression system: Vibrio cholerae

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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

2 mentions without citation

Association analyses of large-scale glycan microarray data reveal novel host-specific substructures in influenza A virus binding glycans.
Zhao et al. (2015)
1 more