8OW8

Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium

8OW8 の概要

• エントリーDOI: 10.2210/pdb8ow8/pdb
• 分子名称: Botulinum-like toxin eBoNT/J light chain, ZINC ION, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: botulinum neurotoxin, homologue, enterococcus faecium, toxin
• 由来する生物種: Enterococcus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51211.29

構造登録者

Gregory, K.S.,Acharya, K.R.,Liu, S.M. (登録日: 2023-04-27, 公開日: 2023-08-30, 最終更新日: 2023-09-06)

主引用文献

Gregory, K.S.,Hall, P.R.,Onuh, J.P.,Mojanaga, O.O.,Liu, S.M.,Acharya, K.R.
Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium : Potential Insights into Substrate Recognition.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: neurotoxins (BoNTs) are the most potent toxins known, causing the deadly disease botulism. They function through Zn-dependent endopeptidase cleavage of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, preventing vesicular fusion and subsequent neurotransmitter release from motor neurons. Several serotypes of BoNTs produced by (BoNT/A-/G and/X) have been well-characterised over the years. However, a BoNT-like gene (homologue of BoNT) was recently identified in the non-clostridial species, which is the leading cause of hospital-acquired multi-drug resistant infections. Here, we report the crystal structure of the catalytic domain of a BoNT homologue from (LC/En) at 2.0 Å resolution. Detailed structural analysis in comparison with the full-length BoNT/En AlphaFold2-predicted structure, LC/A (from BoNT/A), and LC/F (from BoNT/F) revealed putative subsites and exosites (including loops 1-5) involved in recognition of LC/En substrates. LC/En also appears to possess a conserved autoproteolytic cleavage site whose function is yet to be established.

PubMed: 37628902
DOI: 10.3390/ijms241612721

実験手法

X-RAY DIFFRACTION (2 Å)