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| | <StructureSection load='6rim' size='340' side='right'caption='[[6rim]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='6rim' size='340' side='right'caption='[[6rim]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rim]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RIM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rim]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Weissella_oryzae Weissella oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RIM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span></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=6rim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rim OCA], [https://pdbe.org/6rim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rim RCSB], [https://www.ebi.ac.uk/pdbsum/6rim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rim ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rim OCA], [http://pdbe.org/6rim PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rim RCSB], [http://www.ebi.ac.uk/pdbsum/6rim PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rim ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BXWO_WEIOS BXWO_WEIOS]] When overexpressed the N-terminus (residues 1-476) cleaves rat synaptobrevin-2/VAMP2 between '89-Trp-|-Trp-90' in vitro. This releases the cytoplasmic domain of VAMP2 from the synaptic vesicle membrane, which would prevent the assembly of the trans-SNARE complex on the membrane and thus prevent vesicle-target membrane fusion and neurotransmitter release (PubMed:27443638).<ref>PMID:27443638</ref> | + | [https://www.uniprot.org/uniprot/BXWO_WEIOS BXWO_WEIOS] When overexpressed the N-terminus (residues 1-476) cleaves rat synaptobrevin-2/VAMP2 between '89-Trp-|-Trp-90' in vitro. This releases the cytoplasmic domain of VAMP2 from the synaptic vesicle membrane, which would prevent the assembly of the trans-SNARE complex on the membrane and thus prevent vesicle-target membrane fusion and neurotransmitter release (PubMed:27443638).<ref>PMID:27443638</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bontoxilysin]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kosenina, S]] | + | [[Category: Weissella oryzae]] |
| - | [[Category: Masuyer, G]] | + | [[Category: Kosenina S]] |
| - | [[Category: Stenmark, P]] | + | [[Category: Masuyer G]] |
| - | [[Category: Botulinum neurotoxin]] | + | [[Category: Stenmark P]] |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Zinc endopeptidase]]
| + | |
| Structural highlights
Function
BXWO_WEIOS When overexpressed the N-terminus (residues 1-476) cleaves rat synaptobrevin-2/VAMP2 between '89-Trp-|-Trp-90' in vitro. This releases the cytoplasmic domain of VAMP2 from the synaptic vesicle membrane, which would prevent the assembly of the trans-SNARE complex on the membrane and thus prevent vesicle-target membrane fusion and neurotransmitter release (PubMed:27443638).[1]
Publication Abstract from PubMed
Botulinum neurotoxins (BoNTs) are the most potent toxins known. So far, eight serotypes have been identified that all act as zinc-dependent endopeptidases targeting SNARE proteins and inhibiting the release of neurotransmitters. Recently, the first botulinum toxin-like protein was identified outside the Clostridial genus, designated BoNT/Wo in the genome of Weissella oryzae. Here, we report the 1.6 A X-ray crystal structure of the light chain of BoNT/Wo (LC/Wo). LC/Wo presents the core fold common to BoNTs but has an unusually wide, open, and negatively charged catalytic pocket, with an additional Ca(2+) ion besides the zinc ion and a unique ss-hairpin motif. The structural information will help establish the substrate profile of BoNT/Wo and help our understanding of how BoNT evolved. This article is protected by copyright. All rights reserved.
Crystal structure of the catalytic domain of the Weissela oryzae botulinum-like toxin.,Kosenina S, Masuyer G, Zhang S, Dong M, Stenmark P FEBS Lett. 2019 May 20. doi: 10.1002/1873-3468.13446. PMID:31111466[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zornetta I, Azarnia Tehran D, Arrigoni G, Anniballi F, Bano L, Leka O, Zanotti G, Binz T, Montecucco C. The first non Clostridial botulinum-like toxin cleaves VAMP within the juxtamembrane domain. Sci Rep. 2016 Jul 22;6:30257. doi: 10.1038/srep30257. PMID:27443638 doi:http://dx.doi.org/10.1038/srep30257
- ↑ Kosenina S, Masuyer G, Zhang S, Dong M, Stenmark P. Crystal structure of the catalytic domain of the Weissela oryzae botulinum-like toxin. FEBS Lett. 2019 May 20. doi: 10.1002/1873-3468.13446. PMID:31111466 doi:http://dx.doi.org/10.1002/1873-3468.13446
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