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Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium
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Structural highlights
FunctionBXJ_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
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This page was last modified 09:16, 30 August 2023.