Summary for 6TWP
Entry DOI | 10.2210/pdb6twp/pdb |
Descriptor | Botulinum neurotoxin A5, CHLORIDE ION (3 entities in total) |
Functional Keywords | binding domain, botulinum neurotoxin, toxin |
Biological source | Clostridium botulinum |
Total number of polymer chains | 1 |
Total formula weight | 50757.88 |
Authors | Davies, J.R.,Acharya, K.R. (deposition date: 2020-01-13, release date: 2020-07-22, Last modification date: 2024-01-24) |
Primary citation | Davies, J.R.,Britton, A.,Liu, S.M.,Acharya, K.R. High-resolution crystal structures of the botulinum neurotoxin binding domains from subtypes A5 and A6. Febs Open Bio, 10:1474-1481, 2020 Cited by PubMed Abstract: Clostridium botulinum neurotoxins (BoNTs) cause flaccid paralysis through inhibition of acetylcholine release from motor neurons; however, at tiny doses, this property is exploited for use as a therapeutic. Each member of the BoNT family of proteins consists of three distinct domains: a binding domain that targets neuronal cell membranes (H ), a translocation domain (H ) and a catalytic domain (LC). Here, we present high-resolution crystal structures of the binding domains of BoNT subtypes/A5 (H /A5) and/A6 (H /A6). These structures show that the core fold identified in other subtypes is maintained, but with subtle differences at the expected receptor-binding sites. PubMed: 32654405DOI: 10.1002/2211-5463.12931 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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