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.
| Original language | English |
|---|---|
| Pages (from-to) | 1403-1410 |
| Number of pages | 8 |
| Journal | FEBS Letters |
| Volume | 593 |
| Issue number | 12 |
| Early online date | 31 May 2019 |
| DOIs | |
| Publication status | Published - 1 Jun 2019 |
Keywords
- botulinum neurotoxin
- Weissella oryzae
- X-ray crystallography
- zinc endopeptidase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Crystal structure of the catalytic domain of the Weissella oryzae botulinum-like toxin. / Košenina, Sara; Masuyer, Geoffrey; Zhang, Sicai; Dong, Min; Stenmark, Pål.
In: FEBS Letters, Vol. 593, No. 12, 01.06.2019, p. 1403-1410.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystal structure of the catalytic domain of the Weissella oryzae botulinum-like toxin
AU - Košenina, Sara
AU - Masuyer, Geoffrey
AU - Zhang, Sicai
AU - Dong, Min
AU - Stenmark, Pål
PY - 2019/6/1
Y1 - 2019/6/1
N2 - 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.
AB - 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.
KW - botulinum neurotoxin
KW - Weissella oryzae
KW - X-ray crystallography
KW - zinc endopeptidase
UR - http://www.scopus.com/inward/record.url?scp=85066877867&partnerID=8YFLogxK
U2 - 10.1002/1873-3468.13446
DO - 10.1002/1873-3468.13446
M3 - Article
C2 - 31111466
AN - SCOPUS:85066877867
VL - 593
SP - 1403
EP - 1410
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 12
ER -