5mk6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the receptor-binding domain of botulinum neurotoxin A1 (crystal form 1)== | |
| - | + | <StructureSection load='5mk6' size='340' side='right' caption='[[5mk6]], [[Resolution|resolution]] 1.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5mk6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MK6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MK6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | [[Category: | + | <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> |
| - | [[Category: Acharya, K | + | <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=5mk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mk6 OCA], [http://pdbe.org/5mk6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mk6 RCSB], [http://www.ebi.ac.uk/pdbsum/5mk6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mk6 ProSAT]</span></td></tr> |
| - | [[Category: Davies, J | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_CLOBO]] 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bontoxilysin]] | ||
| + | [[Category: Acharya, K R]] | ||
| + | [[Category: Davies, J R]] | ||
| + | [[Category: Bacterial]] | ||
| + | [[Category: Beta trefoil fold]] | ||
| + | [[Category: Jelly roll fold]] | ||
| + | [[Category: Toxin]] | ||
| + | [[Category: Toxin receptor binding domain]] | ||
Revision as of 06:28, 28 March 2018
Crystal structure of the receptor-binding domain of botulinum neurotoxin A1 (crystal form 1)
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