|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6tfj' size='340' side='right'caption='[[6tfj]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='6tfj' size='340' side='right'caption='[[6tfj]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tfj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6TFJ FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vip3LB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1428 "Bacillus cereus var. thuringiensis" Smith et al. 1952])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tfj OCA], [http://pdbe.org/6tfj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tfj RCSB], [http://www.ebi.ac.uk/pdbsum/6tfj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tfj ProSAT]</span></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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q58XI2_BACTU Q58XI2_BACTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus cereus var. thuringiensis smith et al. 1952]] | + | [[Category: Bacillus thuringiensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arias-Palomo, E]] | + | [[Category: Arias-Palomo E]] |
| - | [[Category: Bel, Y]] | + | [[Category: Bel Y]] |
| - | [[Category: Casino, P]] | + | [[Category: Casino P]] |
| - | [[Category: Ferre, J]] | + | [[Category: Ferre J]] |
| - | [[Category: Huesa, J]] | + | [[Category: Huesa J]] |
| - | [[Category: Nunez-Ramirez, R]] | + | [[Category: Nunez-Ramirez R]] |
| - | [[Category: Beta prism]]
| + | |
| - | [[Category: Insecticidal protein]]
| + | |
| - | [[Category: Protoxin]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Vip3]]
| + | |
| - | [[Category: Vip3aa]]
| + | |
| Structural highlights
Function
Q58XI2_BACTU
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nunez-Ramirez R, Huesa J, Bel Y, Ferre J, Casino P, Arias-Palomo E. Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis. Nat Commun. 2020 Aug 7;11(1):3974. doi: 10.1038/s41467-020-17758-5. PMID:32769995 doi:http://dx.doi.org/10.1038/s41467-020-17758-5
|
