6F0P
Botulinum neurotoxin A4 Hc domain
Summary for 6F0P
| Entry DOI | 10.2210/pdb6f0p/pdb |
| Descriptor | Neurotoxin type A, NICKEL (II) ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | botulinum neurotoxin a4 subtype, a4, binding domain, hc domain, toxin |
| Biological source | Clostridium botulinum |
| Total number of polymer chains | 1 |
| Total formula weight | 51547.04 |
| Authors | Davies, J.R.,Rees, J.,Liu, S.M.,Acharya, K.R. (deposition date: 2017-11-20, release date: 2018-01-10, Last modification date: 2024-11-06) |
| Primary citation | Davies, J.R.,Rees, J.,Liu, S.M.,Acharya, K.R. High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains. J. Struct. Biol., 202:113-117, 2018 Cited by PubMed Abstract: Clostridium botulinum neurotoxins (BoNTs) cause the life-threatening condition, botulism. However, while they have the potential to cause serious harm, they are increasingly being utilised for therapeutic applications. BoNTs comprise of seven distinct serotypes termed BoNT/A through BoNT/G, with the most widely characterised being sub-serotype BoNT/A1. Each BoNT consists of three structurally distinct domains, a binding domain (H), a translocation domain (H), and a proteolytic domain (LC). The H domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. Here, we present two high-resolution structures of the binding domain of subtype BoNT/A3 (H/A3) and BoNT/A4 (H/A4) at 1.6 Å and 1.34 Å resolution, respectively. The structures of both proteins share a high degree of similarity to other known BoNT H domains whilst containing some subtle differences, and are of benefit to research into therapeutic neurotoxins with novel characteristics. PubMed: 29288126DOI: 10.1016/j.jsb.2017.12.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.34 Å) |
Structure validation
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