6f0o

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m (Protected "6f0o" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6f0o is ON HOLD
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==Botulinum neurotoxin A3 Hc domain==
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<StructureSection load='6f0o' size='340' side='right' caption='[[6f0o]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6f0o]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F0O 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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene></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='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=6f0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f0o OCA], [http://pdbe.org/6f0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f0o RCSB], [http://www.ebi.ac.uk/pdbsum/6f0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f0o ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Clostridium botulinum neurotoxins (BoNTs) cause the life-threatening condition, botulism. However, while they have the potential to cause serious harm, they are increasingly being utilised for therapeutic applications. BoNTs comprise of seven distinct serotypes termed BoNT/A through BoNT/G, with the most widely characterised being sub-serotype BoNT/A1. Each BoNT consists of three structurally distinct domains, a binding domain (HC), a translocation domain (HN), and a proteolytic domain (LC). The HC domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. Here, we present two high-resolution structures of the binding domain of subtype BoNT/A3 (HC/A3) and BoNT/A4 (HC/A4) at 1.6A and 1.34A resolution, respectively. The structures of both proteins share a high degree of similarity to other known BoNT HC domains whilst containing some subtle differences, and are of benefit to research into therapeutic neurotoxins with novel characteristics.
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Authors: Davies, J.R., Liu, S.M., Acharya, K.R.
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High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains.,Davies JR, Rees J, Liu SM, Acharya KR J Struct Biol. 2017 Dec 26. pii: S1047-8477(17)30233-2. doi:, 10.1016/j.jsb.2017.12.010. PMID:29288126<ref>PMID:29288126</ref>
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Description: Botulinum neurotoxin A3 Hc domain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Acharya, K.R]]
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<div class="pdbe-citations 6f0o" style="background-color:#fffaf0;"></div>
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[[Category: Davies, J.R]]
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== References ==
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[[Category: Liu, S.M]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bontoxilysin]]
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[[Category: Acharya, K R]]
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[[Category: Davies, J R]]
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[[Category: Liu, S M]]
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[[Category: A3]]
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[[Category: Binding domain]]
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[[Category: Botulinum neurotoxin a3 subtype]]
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[[Category: Hc domain]]
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[[Category: Toxin]]

Revision as of 08:33, 10 January 2018

Botulinum neurotoxin A3 Hc domain

6f0o, resolution 1.60Å

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