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TitleMolecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 3974, Year 2020
Publish dateAug 7, 2020
AuthorsRafael Núñez-Ramírez / Juanjo Huesa / Yolanda Bel / Juan Ferré / Patricia Casino / Ernesto Arias-Palomo /
PubMed AbstractBacillus 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 ...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 Å 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.
External linksNat Commun / PubMed:32769995 / PubMed Central
MethodsEM (single particle)
Resolution2.9 Å
Structure data

10492

6tfj

EMDB-10492, PDB-6tfj:
Vip3Aa protoxin structure
Method: EM (single particle) / Resolution: 2.9 Å

10493

6tfk

EMDB-10493, PDB-6tfk:
Vip3Aa toxin structure
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • bacillus thuringiensis (bacteria)
KeywordsTOXIN / Vip3Aa / protoxin / beta prism / insecticidal protein / Vip3

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