Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology submitted time 2016-05-12
Xu, Chengchen
Meng, Ying
Yu, Ziniu
Sun, Ming
Xu, Chengchen
Chinte, Unmesh
Chen, Lirong
Zhou, Dayong
Rose, John
Adang, Michael J.
Wang, Bi-Cheng
Chinte, Unmesh
Rose, John
Wang, Bi-Cheng
Chinte, Unmesh
Rose, John
Wang, Bi-Cheng
Yao, Qingqing
Bi, Li-Jun
Adang, Michael J.
Abstract： 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 angstrom 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-FFTs). 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. (C) 2015 Elsevier Inc. All rights reserved.
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