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Košenina S, Masuyer G, Zhang S, Dong M, Stenmark P
FEBS Lett 593 (12) 1403-1410 [2019-06-00; online 2019-05-31]
Botulinum 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 Å 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.
Bioinformatics Support for Computational Resources [Service]
Protein Science Facility (PSF) [Service]
PubMed 31111466
DOI 10.1002/1873-3468.13446
Crossref 10.1002/1873-3468.13446
PDB: 6RIM Crystal structure of the catalytic domain of the Weissela oryzae botulinum like toxin