4ISR
Binding domain of Botulinum neurotoxin DC in complex with rat synaptotagmin II
Summary for 4ISR
| Entry DOI | 10.2210/pdb4isr/pdb |
| Related | 4ISQ |
| Descriptor | Neurotoxin, Synaptotagmin-2, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | membrane binding, synaptotagmin and ganglioside binding, toxin |
| Biological source | Clostridium botulinum More |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein: P29101 |
| Total number of polymer chains | 6 |
| Total formula weight | 158917.37 |
| Authors | Berntsson, R.P.-A.,Peng, L.,Svensson, L.M.,Dong, M.,Stenmark, P. (deposition date: 2013-01-17, release date: 2013-08-14, Last modification date: 2024-02-28) |
| Primary citation | Berntsson, R.P.,Peng, L.,Svensson, L.M.,Dong, M.,Stenmark, P. Crystal Structures of Botulinum Neurotoxin DC in Complex with Its Protein Receptors Synaptotagmin I and II. Structure, 21:1602-1611, 2013 Cited by PubMed Abstract: Botulinum neurotoxins (BoNTs) can cause paralysis at exceptionally low concentrations and include seven serotypes (BoNT/A-G). The chimeric BoNT/DC toxin has a receptor binding domain similar to the same region in BoNT/C. However, BoNT/DC does not share protein receptor with BoNT/C. Instead, it shares synaptotagmin (Syt) I and II as receptors with BoNT/B, despite their low sequence similarity. Here, we present the crystal structures of the binding domain of BoNT/DC in complex with the recognition domains of its protein receptors, Syt-I and Syt-II. The structures reveal that BoNT/DC possesses a Syt binding site, distinct from the established Syt-II binding site in BoNT/B. Structure-based mutagenesis further shows that hydrophobic interactions play a key role in Syt binding. The structures suggest that the BoNT/DC ganglioside binding sites are independent of the protein receptor binding site. Our results reveal the remarkable versatility in the receptor recognition of the BoNTs. PubMed: 23932591DOI: 10.1016/j.str.2013.06.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
Download full validation report
