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6TWP

Binding domain of BoNT/A5

This is a non-PDB format compatible entry.
Summary for 6TWP
Entry DOI10.2210/pdb6twp/pdb
DescriptorBotulinum neurotoxin A5, CHLORIDE ION (3 entities in total)
Functional Keywordsbinding domain, botulinum neurotoxin, toxin
Biological sourceClostridium botulinum
Total number of polymer chains1
Total formula weight50757.88
Authors
Davies, J.R.,Acharya, K.R. (deposition date: 2020-01-13, release date: 2020-07-22, Last modification date: 2024-01-24)
Primary citationDavies, 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: 32654405
DOI: 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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