9qce
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==HA70-HA17-HA33 complex from Clostridium botulinum Serotype B1== | |
+ | <StructureSection load='9qce' size='340' side='right'caption='[[9qce]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[9qce]] is a 6 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=9QCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QCE 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]] 2.8Å</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=9qce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qce OCA], [https://pdbe.org/9qce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qce RCSB], [https://www.ebi.ac.uk/pdbsum/9qce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qce ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/B1INQ0_CLOBK B1INQ0_CLOBK] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Botulinum neurotoxin serotype B1 (BoNT/B) is a highly potent neurotoxin and therapeutic agent. Here, we present the structure of the complete 14-subunit (780 kDa) progenitor toxin complex (L-PTC) and of five subcomplexes. The structures show how the toxin interacts with its associated components in their role to protect and deliver BoNT/B across epithelial barriers. Each subcomplex, including the M-PTC, M-PTC-HA70, NTNH-HA70, and HA70 trimer, provides detailed understanding of the assembly mechanism, in which the NTNH-nLoop adopts a unique fold that locks the M-PTC into a central pore formed by HA70. The HA subcomplex presents a tripod architecture with flexible legs that may adapt to the rugged cell surface. Mass photometry reveals the pH dependence of BoNT/B release from the complex which is unexpectedly influenced by the presence of HA70. This study provides the complete L-PTC structure, offering insights into its assemblage and supporting the development of countermeasures and therapeutic applications. | ||
- | + | Structure of the complete 14-subunit botulinum neurotoxin B complex reveals a unique anchoring through the narrow central pore of HA70.,Krc A, Kosenina SP, Nowakowska MB, Masuyer G, Stenmark P Sci Adv. 2025 Aug 29;11(35):eadx5058. doi: 10.1126/sciadv.adx5058. Epub 2025 Aug , 27. PMID:40864696<ref>PMID:40864696</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 9qce" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Clostridium botulinum]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Krc A]] | ||
+ | [[Category: Masuyer G]] | ||
+ | [[Category: Persson Kosenina S]] | ||
+ | [[Category: Stenmark P]] |
Current revision
HA70-HA17-HA33 complex from Clostridium botulinum Serotype B1
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