5MK6

Crystal structure of the receptor-binding domain of botulinum neurotoxin A1 (crystal form 1)

Summary for 5MK6

• Entry DOI: 10.2210/pdb5mk6/pdb
• Descriptor: Botulinum neurotoxin type A, SODIUM ION (3 entities in total)
• Functional Keywords: bacterial, toxin, toxin receptor binding domain, jelly roll fold, beta trefoil fold
• Biological source: Clostridium botulinum
• Cellular location: Botulinum neurotoxin A light chain: Secreted. Botulinum neurotoxin A heavy chain: Secreted: P10845
• Total number of polymer chains: 1
• Total formula weight: 50734.40

Authors

Davies, J.R.,Acharya, K.R. (deposition date: 2016-12-02, release date: 2018-03-28, Last modification date: 2024-05-08)

Primary citation

Davies, J.R.,Hackett, G.S.,Liu, S.M.,Acharya, K.R.
High resolution crystal structures of the receptor-binding domain ofClostridium botulinumneurotoxin serotypes A and FA.
PeerJ, 6:e4552-e4552, 2018

PubMed Abstract: The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (H) and a receptor-binding domain (H). Here we report the crystal structure of H/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our H/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of H/A1. This may have implications for receptor-binding and future recombinant toxin production.

PubMed: 29576992
DOI: 10.7717/peerj.4552

Experimental method

X-RAY DIFFRACTION (1.45 Å)