8OW8
Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium
Summary for 8OW8
| Entry DOI | 10.2210/pdb8ow8/pdb |
| Descriptor | Botulinum-like toxin eBoNT/J light chain, ZINC ION, PHOSPHATE ION, ... (6 entities in total) |
| Functional Keywords | botulinum neurotoxin, homologue, enterococcus faecium, toxin |
| Biological source | Enterococcus |
| Total number of polymer chains | 1 |
| Total formula weight | 51211.29 |
| Authors | Gregory, K.S.,Acharya, K.R.,Liu, S.M. (deposition date: 2023-04-27, release date: 2023-08-30, Last modification date: 2023-09-06) |
| Primary citation | 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 Cited by 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: 37628902DOI: 10.3390/ijms241612721 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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