Flexibility Analysis of Bacillus thuringiensis Cry1Aa.

Xin Min Zhao; Li Qiu Xia; Xiao Ping Yang; Xiao Yun Peng

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Flexibility Analysis of Bacillus thuringiensis Cry1Aa.

Author: Xin Min ZHAO ^{1
,

2} ; Li Qiu XIA ³ ; Xiao Ping YANG ¹ ; Xiao Yun PENG ⁴
Author Information

1. Department of Chemistry and Environmental Engineering, Hunan City University, Yiyang 413000, Hunan, China
2. Key Laboratory of Microbial Molecular Biology of Hunan Province, College of Life Science, Hunan Normal University, Changsha 410081, Hunan, China.
3. Key Laboratory of Microbial Molecular Biology of Hunan Province, College of Life Science, Hunan Normal University, Changsha 410081, Hunan, China.
4. Department of Chemistry and Environmental Engineering, Hunan City University, Yiyang 413000, Hunan, China.
Publication Type:Journal Article
Keywords: Bacillus thuringiensis; Constraint Network Analysis; Cry1Aa; Flexibility; NMSim
MeSH: Bacillus thuringiensis; Bacterial Proteins; chemistry; genetics; metabolism; Cluster Analysis; Computer Simulation; Endotoxins; chemistry; genetics; metabolism; Entropy; Hemolysin Proteins; chemistry; genetics; metabolism; Models, Structural; Mutation; Protein Conformation; Protein Unfolding; Software; Temperature
From: Biomedical and Environmental Sciences 2015;28(9):634-641
CountryChina
Language:English
Abstract:
OBJECTIVETo investigate the flexibility and mobility of the Bacillus thuringiensis toxin Cry1Aa.
METHODSThe graph theory-based program Constraint Network Analysis and normal mode-based program NMsim were used to analyze the global and local flexibility indices as well as the fluctuation of individual residues in detail.
RESULTSThe decrease in Cry1Aa network rigidity with the increase of temperature was evident. Two phase transition points in which the Cry1Aa structure lost rigidity during the thermal simulation were identified. Two rigid clusters were found in domains I and II. Weak spots were found in C-terminal domain III. Several flexible regions were found in all three domains; the largest residue fluctuation was present in the apical loop2 of domain II.
CONCLUSIONAlthough several flexible regions could be found in all the three domains, the most flexible regions were in the apical loops of domain II.