› 1ltt

X-ray diffraction
2.3Å resolution

LACTOSE BINDING TO HEAT-LABILE ENTEROTOXIN REVEALED BY X-RAY CRYSTALLOGRAPHY

Released:
DOI: 10.2210/pdb1ltt/pdb
PDB entry 1ltt coloured by chain, front view.
PDB entry 1ltt coloured by chain, side view.
PDB entry 1ltt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography.
Sixma TK, Pronk SE, Kalk KH, van Zanten BA, Berghuis AM, Hol WG
Nature 355 561-4 (1992)
PMID: 1741035

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139157 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 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: Escherichia coli
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)
Heat-labile enterotoxin A chain Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 21.35 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06717 (Residues: 22-206; Coverage: 77%)
Gene names: eltA, ltpA
Sequence domains: Heat-labile enterotoxin alpha chain
Structure domains: Heat-Labile Enterotoxin, subunit A
Heat-labile enterotoxin A chain Chain: C
Molecule details ›
Chain: C
Length: 41 amino acids
Theoretical weight: 4.95 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06717 (Residues: 214-254; Coverage: 17%)
Gene names: eltA, ltpA
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 119.8Å b: 101.2Å c: 64.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 not available
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin.
Spangler BD. (1992)
26 more

2 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
1 more