6tfk

Vip3Aa toxin structure

spinqualitylabelsall models 6tfk, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tfk is a 4 chain structure with sequence from "bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Related: 6tfj Gene: vip3LB ("Bacillus cereus var. thuringiensis" Smith et al. 1952) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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