6f0p

Publication Abstract from PubMed

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 (HC), a translocation domain (HN), and a proteolytic domain (LC). The HC 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 (HC/A3) and BoNT/A4 (HC/A4) at 1.6A and 1.34A resolution, respectively. The structures of both proteins share a high degree of similarity to other known BoNT HC domains whilst containing some subtle differences, and are of benefit to research into therapeutic neurotoxins with novel characteristics.

High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains.,Davies JR, Rees J, Liu SM, Acharya KR J Struct Biol. 2017 Dec 26. pii: S1047-8477(17)30233-2. doi:, 10.1016/j.jsb.2017.12.010. PMID:29288126^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.