› 3chb

X-ray diffraction
1.25Å resolution

CHOLERA TOXIN B-PENTAMER COMPLEXED WITH GM1 PENTASACCHARIDE

Released:
DOI: 10.2210/pdb3chb/pdb
PDB entry 3chb coloured by chain, front view.
PDB entry 3chb coloured by chain, side view.
PDB entry 3chb coloured by chain, top view.
Source organism: Vibrio cholerae
Primary publication:
The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site.
Merritt EA, Kuhn P, Sarfaty S, Erbe JL, Holmes RK, Hol WG
J Mol Biol 282 1043-59 (1998)
PMID: 9753553

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134384 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Cholera enterotoxin subunit B Chains: D, E, F, G, H
Molecule details ›
Chains: D, E, F, G, H
Length: 104 amino acids
Theoretical weight: 11.77 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli
UniProt:
  • Canonical: P01556 (Residues: 22-124; Coverage: 100%)
Gene names: VC_1456, ctxB, toxB
Sequence domains: Heat-labile enterotoxin beta chain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

Carbohydrate polymer : NEW Components: GAL, NGA, SIA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GAL, NGA, SIA, BGC
Carbohydrate polymer
3 bound ligands:
Ligand GLC 2 x GLC
Ligand UNX 5 x UNX
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 102.124Å b: 66.176Å c: 78.221Å
α: 90° β: 106.33° γ: 90°
R-values:
R R work R free
0.133 not available 0.18
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Membrane traffic and the cellular uptake of cholera toxin.
Lencer et al. (1999)
17 more

28 mentions without citation

Protein Toxins That Utilize Gangliosides as Host Receptors.
Zuverink et al. (2018)
27 more