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Crystal structure of the catalytic domain of the Weissella oryzae botulinum-like toxin
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 52019 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 593, no 12, p. 1403-1410Article in journal (Refereed) Published
Abstract [en]

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 angstrom 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 Ca2+ 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.

Place, publisher, year, edition, pages
2019. Vol. 593, no 12, p. 1403-1410
Keywords [en]
botulinum neurotoxin, Weissella oryzae, X-ray crystallography, zinc endopeptidase
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-170881DOI: 10.1002/1873-3468.13446ISI: 000472673700013PubMedID: 31111466OAI: oai:DiVA.org:su-170881DiVA, id: diva2:1338531
Available from: 2019-07-23 Created: 2019-07-23 Last updated: 2019-07-23Bibliographically approved

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Košenina, SaraMasuyer, GeoffreyStenmark, Pål
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