4pkm

Crystal Structure of Bacillus thuringiensis Cry51Aa1 Protoxin at 1.65 Angstroms Resolution

spinqualitylabelsall models 4pkm, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pkm is a 1 chain structure with sequence from Bacillus thuringiensis F14-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: GLY, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A7IZR5_BACTU Publication Abstract from PubMed The structures of several Bacillus thuringiensis (Bt) insecticidal crystal proteins have been determined by crystallographic methods and a close relationship has been explicated between specific toxicities and conserved three-dimensional architectures. In this study, as a representative of the coleopteran- and hemipteran-specific Cry51A group, the complete structure of Cry51Aa1 protoxin has been determined by X-ray crystallography at 1.65 A resolution. This is the first report of a coleopteran-active Bt insecticidal toxin with high structural similarity to the aerolysin-type beta-pore forming toxins (beta-PFTs). Moreover, study of featured residues and structural elements reveal their possible roles in receptor binding and pore formation events. This study provides new insights into the action of aerolysin-type beta-PFTs from a structural perspective, and could be useful for the control of coleopteran and hemipteran insect pests in agricultures. Crystal structure of Cry51Aa1: A potential novel insecticidal aerolysin-type beta-pore-forming toxin from Bacillus thuringiensis.,Xu C, Chinte U, Chen L, Yao Q, Meng Y, Zhou D, Bi LJ, Rose J, Adang MJ, Wang BC, Yu Z, Sun M Biochem Biophys Res Commun. 2015 May 7. pii: S0006-291X(15)00758-5. doi:, 10.1016/j.bbrc.2015.04.068. PMID:25957471 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA