6yrg

Vip3Bc1 tetramer in processed, activated state

spinqualitylabelsall models 6yrg, resolution 7.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yrg is a 4 chain structure with sequence from Bacillus thuringiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A290WPI2_BACTU Publication Abstract from PubMed Insect pests are a major cause of crop losses worldwide, with an estimated economic cost of $470 billion annually. Biotechnological tools have been introduced to control such insects without the need for chemical pesticides; for instance, the development of transgenic plants harbouring genes encoding insecticidal proteins. The Vip3 (vegetative insecticidal protein 3) family proteins from Bacillus thuringiensis convey toxicity to species within the Lepidoptera, and have wide potential applications in commercial agriculture. Vip3 proteins are proposed to exert their insecticidal activity through pore formation, though to date there is no mechanistic description of how this occurs on the membrane. Here we present cryo-EM structures of a Vip3 family toxin in both inactive and activated forms in conjunction with structural and functional data on toxin-membrane interactions. Together these data demonstrate that activated Vip3Bc1 complex is able to insert into membranes in a highly efficient manner, indicating that receptor binding is the likely driver of Vip3 specificity. Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane.,Byrne MJ, Iadanza MG, Perez MA, Maskell DP, George RM, Hesketh EL, Beales PA, Zack MD, Berry C, Thompson RF Nat Commun. 2021 May 14;12(1):2791. doi: 10.1038/s41467-021-23146-4. PMID:33990582 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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