6v1v | pdb_00006v1v

VIP3B (VIP3B_2160) adapted for crystallization

spinqualitylabelsall models 6v1v, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6v1v 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. Gene: vip3Bc1 ("Bacillus cereus var. thuringiensis" Smith et al. 1952) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Vegetatively expressed insecticidal proteins (VIPs) produced by Bacillus thuringiensis fall into several classes of which the third, VIP3, is known for their activity against several key Lepidopteran pests of commercial broad acre crops and because their mode of action does not overlap with that of crystalline insecticidal proteins. The details of the VIP3 structure and mode of action have remained obscure for the quarter century that has passed since their discovery. In the present article, we report the first crystal structure of a full-length VIP3 protein. Crystallization of this target required multiple rounds of construct optimization and screening-over 200 individual sequences were expressed and tested. This protein adopts a novel global fold that combines domains with hitherto unreported topology and containing elements seemingly borrowed from carbohydrate-binding domains, lectins, or from other insecticidal proteins. Crystal structure of a Vip3B family insecticidal protein reveals a new fold and a unique tetrameric assembly.,Zheng M, Evdokimov AG, Moshiri F, Lowder C, Haas J Protein Sci. 2019 Dec 16. doi: 10.1002/pro.3803. PMID:31840313 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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