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

Sara Košenina, Geoffrey Masuyer, Sicai Zhang, Min Dong, Pål Stenmark

Research output: Contribution to journalArticlepeer-review

7 Citations (SciVal)


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.

Original languageEnglish
Pages (from-to)1403-1410
Number of pages8
JournalFEBS Letters
Issue number12
Early online date31 May 2019
Publication statusPublished - 1 Jun 2019


  • botulinum neurotoxin
  • Weissella oryzae
  • X-ray crystallography
  • zinc endopeptidase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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