8byp: Difference between revisions

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New page: '''Unreleased structure''' The entry 8byp is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 8byp is ON HOLD
==Botulinum neurotoxin serotype X in complex with NTNH/X==
<StructureSection load='8byp' size='340' side='right'caption='[[8byp]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8byp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BYP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.12&#8491;</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=8byp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8byp OCA], [https://pdbe.org/8byp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8byp RCSB], [https://www.ebi.ac.uk/pdbsum/8byp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8byp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Botulinum neurotoxins (BoNTs) are the most potent toxins known and are used to treat an increasing number of medical disorders. All BoNTs are naturally co-expressed with a protective partner protein (NTNH) with which they form a 300 kDa complex, to resist acidic and proteolytic attack from the digestive tract. We have previously identified a new botulinum neurotoxin serotype, BoNT/X, that has unique and therapeutically attractive properties. We present the cryo-EM structure of the BoNT/X-NTNH/X complex at 3.1 A resolution. Unexpectedly, the BoNT/X complex is stable and protease resistant at both neutral and acidic pH and disassembles only in alkaline conditions. Using the stabilizing effect of NTNH, we isolated BoNT/X and showed that it has very low potency both in vitro and in vivo . Given the high catalytic activity and translocation efficacy of BoNT/X, low activity of the full toxin is likely due to the receptor-binding domain, which presents weak ganglioside binding and exposed hydrophobic surfaces.


Authors:  
Structure and activity of botulinum neurotoxin X.,Martinez-Carranza M, Skerlova J, Lee PG, Zhang J, Burgin D, Elliott M, Philippe J, Donald S, Hornby F, Henriksson L, Masuyer G, Beard M, Dong M, Stenmark P bioRxiv [Preprint]. 2023 Jan 11:2023.01.11.523524. doi: , 10.1101/2023.01.11.523524. PMID:36712025<ref>PMID:36712025</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8byp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium botulinum]]
[[Category: Large Structures]]
[[Category: Martinez-Carranza M]]
[[Category: Skerlova J]]
[[Category: Stenmark P]]

Latest revision as of 09:30, 17 October 2024

Botulinum neurotoxin serotype X in complex with NTNH/X

8byp, resolution 3.12Å

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