Structural highlights
Function
BXJ_ENTS3 Strongly resembles a botulinum-type toxin, with the appropriate domains and residues to have proteolytic function, although its C-terminus (which binds to a eukaryotic host cell) is different enough from clostrial botulinum toxins that it might bind another cell target (PubMed:29323697). Might be a precursor of a toxin that binds to an unknown eukaryotic cell receptor(s), and be taken up into the host cell via the endocytic pathway. When the pH of the putative toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the heavy chain forms pores that allows the light chain to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and light chain cleaves its target protein (By similarity).[UniProtKB:P0DPI0][1]
References
- ↑ Brunt J, Carter AT, Stringer SC, Peck MW. Identification of a novel botulinum neurotoxin gene cluster in Enterococcus. FEBS Lett. 2018 Feb;592(3):310-317. PMID:29323697 doi:10.1002/1873-3468.12969