9QC8
BoNT-NTNH-HA70 complex from Clostridium botulinum Serotype B1
This is a non-PDB format compatible entry.
Summary for 9QC8
| Entry DOI | 10.2210/pdb9qc8/pdb |
| EMDB information | 52666 53006 |
| Descriptor | Botulinum neurotoxin type B, Non-toxic non-hemagglutinin component, Hemagglutinin component HA70 (3 entities in total) |
| Functional Keywords | progenitor-toxin complex, botulinum neurotoxin, hemagglutinin, toxin |
| Biological source | Clostridium botulinum More |
| Total number of polymer chains | 5 |
| Total formula weight | 505051.87 |
| Authors | Krc, A.,Persson Kosenina, S.,Masuyer, G.,Stenmark, P. (deposition date: 2025-03-04, release date: 2025-09-10) |
| Primary citation | Krc, A.,Kosenina, S.P.,Nowakowska, M.B.,Masuyer, G.,Stenmark, P. Structure of the complete 14-subunit botulinum neurotoxin B complex reveals a unique anchoring through the narrow central pore of HA70. Sci Adv, 11:eadx5058-eadx5058, 2025 Cited by PubMed Abstract: Botulinum neurotoxin serotype B1 (BoNT/B) is a highly potent neurotoxin and therapeutic agent. Here, we present the structure of the complete 14-subunit (780 kDa) progenitor toxin complex (L-PTC) and of five subcomplexes. The structures show how the toxin interacts with its associated components in their role to protect and deliver BoNT/B across epithelial barriers. Each subcomplex, including the M-PTC, M-PTC-HA70, NTNH-HA70, and HA70 trimer, provides detailed understanding of the assembly mechanism, in which the NTNH-nLoop adopts a unique fold that locks the M-PTC into a central pore formed by HA70. The HA subcomplex presents a tripod architecture with flexible legs that may adapt to the rugged cell surface. Mass photometry reveals the pH dependence of BoNT/B release from the complex which is unexpectedly influenced by the presence of HA70. This study provides the complete L-PTC structure, offering insights into its assemblage and supporting the development of countermeasures and therapeutic applications. PubMed: 40864696DOI: 10.1126/sciadv.adx5058 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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