Crystal structure of the catalytic domain of the Weissela oryzae botulinum-like toxin
Košenina, Sara ; Masuyer, Geoffrey ; Zhang, Sicai ; Dong, Min and Stenmark, Pål LU
(2019)
In FEBS Letters
593(12).
p.1403-1410
- 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... (More)
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.
(Less)
- author
- Košenina, Sara
; Masuyer, Geoffrey
; Zhang, Sicai
; Dong, Min
and Stenmark, Pål
LU
- organization
- publishing date
- 2019-05-20
- type
- Contribution to journal
- publication status
- published
- subject
- in
- FEBS Letters
- volume
- 593
- issue
- 12
- pages
- 1403 - 1410
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:31111466
- scopus:85066877867
- ISSN
- 1873-3468
- DOI
- 10.1002/1873-3468.13446
- language
- English
- LU publication?
- yes
- additional info
- This article is protected by copyright. All rights reserved.
- id
- 98aab847-0fb5-4121-a28a-769bb888387a
- date added to LUP
- 2019-05-28 07:24:29
- date last changed
- 2024-04-30 10:23:31
@article{98aab847-0fb5-4121-a28a-769bb888387a,
abstract = {{<p>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.</p>}},
author = {{Košenina, Sara and Masuyer, Geoffrey and Zhang, Sicai and Dong, Min and Stenmark, Pål}},
issn = {{1873-3468}},
language = {{eng}},
month = {{05}},
number = {{12}},
pages = {{1403--1410}},
publisher = {{Wiley-Blackwell}},
series = {{FEBS Letters}},
title = {{Crystal structure of the catalytic domain of the Weissela oryzae botulinum-like toxin}},
url = {{http://dx.doi.org/10.1002/1873-3468.13446}},
doi = {{10.1002/1873-3468.13446}},
volume = {{593}},
year = {{2019}},
}