期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 462, 期 3, 页码 184-189出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.04.068
关键词
Bacillus thuringiensis; Crystal structure; Insecticidal; Pore-forming toxin
资金
- State Key Program of National Natural Science of China [30930004, 31170047]
- National High Technology Research and Development Program (863) of China [2011AA10A203]
- China 948 Program of Ministry of Agriculture [2011-G25]
- Georgia Research Alliance and the University of Georgia Research Foundation
- U. S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
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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