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-Structure paper
タイトル | Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 3974, Year 2020 |
掲載日 | 2020年8月7日 |
著者 | Rafael Núñez-Ramírez / Juanjo Huesa / Yolanda Bel / Juan Ferré / Patricia Casino / Ernesto Arias-Palomo / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:32769995 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.9 Å |
構造データ | EMDB-10492, PDB-6tfj: EMDB-10493, PDB-6tfk: |
化合物 | ChemComp-MG: |
由来 |
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キーワード | TOXIN / Vip3Aa / protoxin / beta prism / insecticidal protein / Vip3 |