View source for 6tfj


==Vip3Aa protoxin structure==
<StructureSection load='6tfj' size='340' side='right'caption='[[6tfj]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tfj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TFJ 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]] 2.9&#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=6tfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tfj OCA], [https://pdbe.org/6tfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tfj RCSB], [https://www.ebi.ac.uk/pdbsum/6tfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tfj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q58XI2_BACTU Q58XI2_BACTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacillus thuringiensis Vip3 (Vegetative Insecticidal Protein 3) toxins are widely used in biotech crops to control Lepidopteran pests. These proteins are produced as inactive protoxins that need to be activated by midgut proteases to trigger cell death. However, little is known about their three-dimensional organization and activation mechanism at the molecular level. Here, we have determined the structures of the protoxin and the protease-activated state of Vip3Aa at 2.9 A using cryo-electron microscopy. The reconstructions show that the protoxin assembles into a pyramid-shaped tetramer with the C-terminal domains exposed to the solvent and the N-terminal region folded into a spring-loaded apex that, after protease activation, drastically remodels into an extended needle by a mechanism akin to that of influenza haemagglutinin. These results provide the molecular basis for Vip3 activation and function, and serves as a strong foundation for the development of more efficient insecticidal proteins.

Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis.,Nunez-Ramirez R, Huesa J, Bel Y, Ferre J, Casino P, Arias-Palomo E Nat Commun. 2020 Aug 7;11(1):3974. doi: 10.1038/s41467-020-17758-5. PMID:32769995<ref>PMID:32769995</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tfj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus thuringiensis]]
[[Category: Large Structures]]
[[Category: Arias-Palomo E]]
[[Category: Bel Y]]
[[Category: Casino P]]
[[Category: Ferre J]]
[[Category: Huesa J]]
[[Category: Nunez-Ramirez R]]