3qw5: Difference between revisions

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==Crystal structure of the protease domain of Botulinum Neurotoxin Serotype A with a peptide inhibitor RRGF==
==Crystal structure of the protease domain of Botulinum Neurotoxin Serotype A with a peptide inhibitor RRGF==
<StructureSection load='3qw5' size='340' side='right' caption='[[3qw5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3qw5' size='340' side='right'caption='[[3qw5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qw5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum_a_str._hall Clostridium botulinum a str. hall]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QW5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qw5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum_A_str._Hall Clostridium botulinum A str. Hall]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QW5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.6&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">[[3bwi|3bwi]], [[3c88|3c88]], [[3c89|3c89]], [[3c8a|3c8a]], [[3c8b|3c8b]], [[3dda|3dda]], [[3ddb|3ddb]], [[3qw6|3qw6]], [[3qw7|3qw7]], [[3qw8|3qw8]]</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=3qw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw5 OCA], [https://pdbe.org/3qw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qw5 RCSB], [https://www.ebi.ac.uk/pdbsum/3qw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qw5 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botA, CBO0806, CLC_0862 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=441771 Clostridium botulinum A str. Hall])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qw5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qw5 RCSB], [http://www.ebi.ac.uk/pdbsum/3qw5 PDBsum]</span></td></tr>
</table>
</table>
== 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.
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3qw5" style="background-color:#fffaf0;"></div>
==See Also==
*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bontoxilysin]]
[[Category: Clostridium botulinum A str. Hall]]
[[Category: Clostridium botulinum a str. hall]]
[[Category: Large Structures]]
[[Category: Kumaran, D]]
[[Category: Kumaran D]]
[[Category: Swaminathan, S]]
[[Category: Swaminathan S]]
[[Category: Bio-warfare agent]]
[[Category: Endopeptidase]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Protease]]
[[Category: Secreted]]
[[Category: Snap25]]
[[Category: Syntaxin]]
[[Category: Transmembrane]]

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