Article
Residue 544 in domain III of the Bacillus thuringiensis Cry1Ac toxin is involved in protein structure stability.
The protein journal - 1 Aug 2010
Liu Yong Le, Wang Qin Yun, Wang Fa Xiang, Ding Xue Zhi, Xia Li Qiu
Abstract excerpt
A unique residue W544 in the beta18-beta19 loop of the Bacillus thuringiensis Cry1Ac toxin has been implicated in its toxicity. In this study, the effects of mutations at this residue on protein stability during protease treatment, UV irradiation, and preservation were examined. Residue 544 of Cry1Ac was involved in maintaining structural stability, and substitution of a polar group at this position was...
Topics
- Bacillus thuringiensis
- Bacillus thuringiensis Toxins
- Bacterial Proteins
- Electrophoresis, Polyacrylamide Gel
- Endotoxins
- Hemolysin Proteins
- Microscopy, Atomic Force
- Models, Molecular
- Mutation
- Protein Stability