4isq: Difference between revisions

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==Binding domain of Botulinum neurotoxin DC in complex with human synaptotagmin I==
==Binding domain of Botulinum neurotoxin DC in complex with human synaptotagmin I==
<StructureSection load='4isq' size='340' side='right' caption='[[4isq]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='4isq' size='340' side='right' caption='[[4isq]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4isq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ISQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ISQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4isq]] is a 6 chain structure with sequence from [http://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=4ISQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ISQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4isr|4isr]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4isr|4isr]]</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=4isq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4isq RCSB], [http://www.ebi.ac.uk/pdbsum/4isq PDBsum]</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=4isq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isq OCA], [http://pdbe.org/4isq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4isq RCSB], [http://www.ebi.ac.uk/pdbsum/4isq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4isq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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 4isq" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium botulinum]]
[[Category: Bacillus botulinus van ermengem 1896]]
[[Category: Berntsson, R P.A]]
[[Category: Berntsson, R P.A]]
[[Category: Dong, M]]
[[Category: Dong, M]]

Revision as of 01:58, 6 August 2016

Binding domain of Botulinum neurotoxin DC in complex with human synaptotagmin IBinding domain of Botulinum neurotoxin DC in complex with human synaptotagmin I

Structural highlights

4isq is a 6 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SYT1_HUMAN] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Publication Abstract from PubMed

Botulinum neurotoxins (BoNTs) can cause paralysis at exceptionally low concentrations and include seven serotypes (BoNT/A-G). The chimeric BoNT/DC toxin has a receptor binding domain similar to the same region in BoNT/C. However, BoNT/DC does not share protein receptor with BoNT/C. Instead, it shares synaptotagmin (Syt) I and II as receptors with BoNT/B, despite their low sequence similarity. Here, we present the crystal structures of the binding domain of BoNT/DC in complex with the recognition domains of its protein receptors, Syt-I and Syt-II. The structures reveal that BoNT/DC possesses a Syt binding site, distinct from the established Syt-II binding site in BoNT/B. Structure-based mutagenesis further shows that hydrophobic interactions play a key role in Syt binding. The structures suggest that the BoNT/DC ganglioside binding sites are independent of the protein receptor binding site. Our results reveal the remarkable versatility in the receptor recognition of the BoNTs.

Crystal Structures of Botulinum Neurotoxin DC in Complex with Its Protein Receptors Synaptotagmin I and II.,Berntsson RP, Peng L, Svensson LM, Dong M, Stenmark P Structure. 2013 Sep 3;21(9):1602-11. doi: 10.1016/j.str.2013.06.026. Epub 2013, Aug 8. PMID:23932591[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Berntsson RP, Peng L, Svensson LM, Dong M, Stenmark P. Crystal Structures of Botulinum Neurotoxin DC in Complex with Its Protein Receptors Synaptotagmin I and II. Structure. 2013 Sep 3;21(9):1602-11. doi: 10.1016/j.str.2013.06.026. Epub 2013, Aug 8. PMID:23932591 doi:http://dx.doi.org/10.1016/j.str.2013.06.026

4isq, resolution 2.65Å

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