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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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.