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==Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium== | |||
<StructureSection load='8ow8' size='340' side='right'caption='[[8ow8]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ow8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus Enterococcus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OW8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ow8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ow8 OCA], [https://pdbe.org/8ow8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ow8 RCSB], [https://www.ebi.ac.uk/pdbsum/8ow8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ow8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BXJ_ENTS3 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]<ref>PMID:29323697</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterococcus]] | |||
[[Category: Large Structures]] | |||
[[Category: Acharya KR]] | |||
[[Category: Gregory KS]] | |||
[[Category: Liu SM]] | |||
Latest revision as of 12:16, 30 August 2023
Crystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faeciumCrystal Structure of the Catalytic Domain of a Botulinum Neurotoxin Homologue from Enterococcus faecium
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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