Structural highlights
Function[BXWO_WEIOS] When overexpressed the N-terminus (residues 1-476) cleaves rat synaptobrevin-2/VAMP2 between '89-Trp-|-Trp-90' in vitro. This releases the cytoplasmic domain of VAMP2 from the synaptic vesicle membrane, which would prevent the assembly of the trans-SNARE complex on the membrane and thus prevent vesicle-target membrane fusion and neurotransmitter release (PubMed:27443638).[1] Publication Abstract from PubMedBotulinum neurotoxins (BoNTs) are the most potent toxins known. So far, eight serotypes have been identified that all act as zinc-dependent endopeptidases targeting SNARE proteins and inhibiting the release of neurotransmitters. Recently, the first botulinum toxin-like protein was identified outside the Clostridial genus, designated BoNT/Wo in the genome of Weissella oryzae. Here, we report the 1.6 A X-ray crystal structure of the light chain of BoNT/Wo (LC/Wo). LC/Wo presents the core fold common to BoNTs but has an unusually wide, open, and negatively charged catalytic pocket, with an additional Ca(2+) ion besides the zinc ion and a unique ss-hairpin motif. The structural information will help establish the substrate profile of BoNT/Wo and help our understanding of how BoNT evolved. This article is protected by copyright. All rights reserved. Crystal structure of the catalytic domain of the Weissela oryzae botulinum-like toxin.,Kosenina S, Masuyer G, Zhang S, Dong M, Stenmark P FEBS Lett. 2019 May 20. doi: 10.1002/1873-3468.13446. PMID:31111466[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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