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6dkk

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==Structure of BoNT==
==Structure of BoNT==
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<StructureSection load='6dkk' size='340' side='right' caption='[[6dkk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='6dkk' size='340' side='right'caption='[[6dkk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6dkk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DKK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6dkk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum_A_str._ATCC_19397 Clostridium botulinum A str. ATCC 19397]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DKK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<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=6dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dkk OCA], [http://pdbe.org/6dkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dkk RCSB], [http://www.ebi.ac.uk/pdbsum/6dkk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dkk ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dkk OCA], [https://pdbe.org/6dkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dkk RCSB], [https://www.ebi.ac.uk/pdbsum/6dkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dkk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6dkk" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6dkk" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bontoxilysin]]
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[[Category: Clostridium botulinum A str. ATCC 19397]]
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[[Category: Jin, R]]
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[[Category: Large Structures]]
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[[Category: Lam, K]]
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[[Category: Jin R]]
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[[Category: Botulinum neurotoxin]]
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[[Category: Lam K]]
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[[Category: Protein translocation]]
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[[Category: Toxin]]
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Current revision

Structure of BoNT

PDB ID 6dkk

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