Crystal structure of the catalytic domain of the Weissela oryzae botulinum-like toxin

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Abstract

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 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. This article is protected by copyright. All rights reserved.

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Authors
Organisations
External organisations
  • Stockholm University
  • Harvard Medical School
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Structural Biology
Original languageEnglish
JournalFEBS Letters
Publication statusE-pub ahead of print - 2019 May 20
Publication categoryResearch
Peer-reviewedYes

Bibliographic note

This article is protected by copyright. All rights reserved.