3dse
From Proteopedia
(Difference between revisions)
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==A potent peptidomimetic inhibitor of botulinum neurotoxin serotype A has a very different conformation than SNAP-25 substrate== | ==A potent peptidomimetic inhibitor of botulinum neurotoxin serotype A has a very different conformation than SNAP-25 substrate== | ||
- | <StructureSection load='3dse' size='340' side='right' caption='[[3dse]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3dse' size='340' side='right'caption='[[3dse]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3dse]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3dse]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DSE FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2isg|2isg]], [[1xtf|1xtf]], [[3ds9|3ds9]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2isg|2isg]], [[1xtf|1xtf]], [[3ds9|3ds9]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botA, CBO0806, CLC_0862 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botA, CBO0806, CLC_0862 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dse OCA], [https://pdbe.org/3dse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dse RCSB], [https://www.ebi.ac.uk/pdbsum/3dse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dse ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/BXA1_CLOBH BXA1_CLOBH]] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
- | *[[Botulinum neurotoxin|Botulinum neurotoxin]] | + | *[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bacillus botulinus van ermengem 1896]] | [[Category: Bacillus botulinus van ermengem 1896]] | ||
[[Category: Bontoxilysin]] | [[Category: Bontoxilysin]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Fenn, T]] | [[Category: Fenn, T]] | ||
[[Category: Zuniga, J E]] | [[Category: Zuniga, J E]] |
Revision as of 08:06, 9 February 2022
A potent peptidomimetic inhibitor of botulinum neurotoxin serotype A has a very different conformation than SNAP-25 substrate
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Categories: Bacillus botulinus van ermengem 1896 | Bontoxilysin | Large Structures | Fenn, T | Zuniga, J E | Botulism | Hydrolase | Inhibition | Membrane | Metal-binding | Metalloprotease | Neuromuscular junction | Neurotoxin | Neurotransmission | Pharmaceutical | Protease | Secreted | Snare | Toxin | Transmembrane | Zinc