7QFQ

Cryo-EM structure of Botulinum neurotoxin serotype B

Summary for 7QFQ

• Entry DOI: 10.2210/pdb7qfq/pdb
• EMDB information: 13947
• Descriptor: Botulinum neurotoxin type B (1 entity in total)
• Functional Keywords: clostridium botulinum, neurotoxin, toxin
• Biological source: Clostridium botulinum
• Total number of polymer chains: 1
• Total formula weight: 153021.92

Authors

Kosenina, S.,Martinez-Carranza, M.,Davies, J.R.,Masuyer, G.,Stenmark, P. (deposition date: 2021-12-06, release date: 2022-01-26, Last modification date: 2024-11-13)

Primary citation

Kosenina, S.,Martinez-Carranza, M.,Davies, J.R.,Masuyer, G.,Stenmark, P.
Structural Analysis of Botulinum Neurotoxins Type B and E by Cryo-EM.
Toxins, 14:-, 2021

PubMed Abstract: Botulinum neurotoxins (BoNTs) are the causative agents of a potentially lethal paralytic disease targeting cholinergic nerve terminals. Multiple BoNT serotypes exist, with types A, B and E being the main cause of human botulism. Their extreme toxicity has been exploited for cosmetic and therapeutic uses to treat a wide range of neuromuscular disorders. Although naturally occurring BoNT types share a common end effect, their activity varies significantly based on the neuronal cell-surface receptors and intracellular SNARE substrates they target. These properties are the result of structural variations that have traditionally been studied using biophysical methods such as X-ray crystallography. Here, we determined the first structures of botulinum neurotoxins using single-particle cryogenic electron microscopy. The maps obtained at 3.6 and 3.7 Å for BoNT/B and /E, respectively, highlight the subtle structural dynamism between domains, and of the binding domain in particular. This study demonstrates how the recent advances made in the field of single-particle electron microscopy can be applied to bacterial toxins of clinical relevance and the botulinum neurotoxin family in particular.

PubMed: 35050991
DOI: 10.3390/toxins14010014

Experimental method

ELECTRON MICROSCOPY (3.6 Å)