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Crystal structure of the catalytic domain of the Weissella oryzae botulinum‐like toxin
Author(s) -
Košenina Sara,
Masuyer Geoffrey,
Zhang Sicai,
Dong Min,
Stenmark Pål
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13446
Subject(s) - chemistry , toxin , crystal structure , clostridium botulinum , biochemistry , crystallography , stereochemistry
Botulinum neurotoxins (Bo NT s) 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 Bo NT /Wo in the genome of Weissella oryzae . Here, we report the 1.6 Å X‐ray crystal structure of the light chain of Bo NT /Wo ( LC /Wo). LC /Wo presents the core fold common to Bo NT s 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 Bo NT /Wo and help our understanding of how Bo NT evolved.