6F0P

Botulinum neurotoxin A4 Hc domain

6F0P の概要

• エントリーDOI: 10.2210/pdb6f0p/pdb
• 分子名称: Neurotoxin type A, NICKEL (II) ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• 機能のキーワード: botulinum neurotoxin a4 subtype, a4, binding domain, hc domain, toxin
• 由来する生物種: Clostridium botulinum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51547.04

構造登録者

Davies, J.R.,Rees, J.,Liu, S.M.,Acharya, K.R. (登録日: 2017-11-20, 公開日: 2018-01-10, 最終更新日: 2024-11-06)

主引用文献

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

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: 29288126
DOI: 10.1016/j.jsb.2017.12.010

実験手法

X-RAY DIFFRACTION (1.34 Å)