7OVW
Binding domain of botulinum neurotoxin E in complex with GD1a
This is a non-PDB format compatible entry.
Summary for 7OVW
| Entry DOI | 10.2210/pdb7ovw/pdb |
| Descriptor | Neurotoxin type E, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-beta-D-galactopyranose, ... (4 entities in total) |
| Functional Keywords | botulinum neurotoxin, ganglioside, toxin receptor, bacterial toxin, carbohydrate binding, toxin |
| Biological source | Clostridium botulinum |
| Total number of polymer chains | 2 |
| Total formula weight | 110494.68 |
| Authors | Masuyer, G.,Stenmark, P. (deposition date: 2021-06-15, release date: 2021-08-11, Last modification date: 2024-01-31) |
| Primary citation | Masuyer, G.,Davies, J.R.,Stenmark, P. Mechanism of Ganglioside Receptor Recognition by Botulinum Neurotoxin Serotype E. Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: The botulinum neurotoxins are potent molecules that are not only responsible for the lethal paralytic disease botulism, but have also been harnessed for therapeutic uses in the treatment of an increasing number of chronic neurological and neuromuscular disorders, in addition to cosmetic applications. The toxins act at the cholinergic nerve terminals thanks to an efficient and specific mechanism of cell recognition which is based on a dual receptor system that involves gangliosides and protein receptors. Binding to surface-anchored gangliosides is the first essential step in this process. Here, we determined the X-ray crystal structure of the binding domain of BoNT/E, a toxin of clinical interest, in complex with its GD1a oligosaccharide receptor. Beyond confirmation of the conserved ganglioside binding site, we identified key interacting residues that are unique to BoNT/E and a significant rearrangement of loop 1228-1237 upon carbohydrate binding. These observations were also supported by thermodynamic measurements of the binding reaction and assessment of ganglioside selectivity by immobilised-receptor binding assays. These results provide a structural basis to understand the specificity of BoNT/E for complex gangliosides. PubMed: 34361086DOI: 10.3390/ijms22158315 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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