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

Crystal structure of the catalytic domain of the Weissella oryzae botulinum-like toxin.
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米魏斯菌肉毒杆菌样毒素催化结构域的晶体结构。

DOI:
10.1002/1873-3468.13446
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发表时间:
2019
期刊:
影响因子:
3.5
通讯作者:
Stenmark,Pål
Stenmark,Pål
中科院分区:
生物学3区
文献类型:
--
作者:
Košenina,Sara;Masuyer,Geoffrey;Zhang,Sicai;Dong,Min;Stenmark,Pål

文献摘要

相似文献

肉毒杆菌神经毒素(BoNT)是已知最有效的毒素。到目前为止,已鉴定出八种血清型,它们都是锌依赖性内肽酶,靶向 SNARE 蛋白并抑制神经递质的释放。最近,第一个肉毒杆菌毒素样蛋白在梭状芽胞杆菌属之外被发现,在米魏斯菌基因组中命名为 BoNT/Wo。在这里,我们报道了 BoNT/Wo (LC/Wo) 轻链的 1.6 Å X 射线晶体结构。 LC/Wo 具有 BoNT 常见的核心折叠,但具有异常宽阔、开放且带负电的催化口袋,除了锌离子外还具有额外的 Ca2+ 离子和独特的 ß-发夹基序。结构信息将有助于建立 BoNT/Wo 的底物概况,并帮助我们了解 BoNT 如何进化。
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 ofWeissella 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.