1ji6 | pdb_00001ji6

CRYSTAL STRUCTURE OF THE INSECTICIDAL BACTERIAL DEL ENDOTOXIN CRY3Bb1 BACILLUS THURINGIENSIS

spinqualitylabelsall models 1ji6, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ji6 is a 1 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. Related: 1dlc Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CR3BB_BACTU] Promotes colloidosmotic lysis by binding to the midgut epithelial cells of Coleoptera. Has moderate level of toxicity to southern corn rootworm. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The coleopteran-active delta-endotoxin Cry3Bb1 from Bacillus thuringiensis (Bt) strain EG7231 is uniquely toxic to Diabrotica undecimpunctata, the Southern corn rootworm, while retaining activity against Leptinotarsa decemlineata, the Colorado potato beetle. The crystal structure of the delta-endotoxin Cry3Bb1 has been refined using data collected to 2.4 A resolution, with a residual R factor of 17.5% and an R(free) of 25.3%. The structure is made up of three domains: I, a seven-helix bundle (residues 64-294); II, a three-sheet domain (residues 295-502); and III, a beta-sandwich domain (residues 503-652). The monomers in the orthorhombic C222(1) crystal lattice form a dimeric quaternary structure across a crystallographic twofold axis, with a channel formed involving interactions between domains I and III. There are 23 hydrogen bonds between the two monomers conferring structural stability on the dimer. It has been demonstrated that Cry3Bb1 and the similar toxin Cry3A form oligomers in solution. The structural results presented here indicate that the interactions between domains I and III could be responsible for the initial higher order structure and have implications for the biological activity of these toxins. There are seven additional single amino-acid residues in the sequence of Cry3Bb1 compared with that of Cry3A; one in domain I, two in domain II and four in domain III, which also shows the largest conformational difference between the two proteins. These changes can be implicated in the selectivity differences noted for these two delta-endotoxins. Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of Bacillus thuringiensis.,Galitsky N, Cody V, Wojtczak A, Ghosh D, Luft JR, Pangborn W, English L Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1101-9. Epub 2001, Jul 23. PMID:11468393 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Delta-endotoxin Pesticidal crystal protein

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