Flexibility Analysis of Bacillus thuringiensis Cry1Aa

ZHAO Xin Min; XIA Li Qiu; YANG Xiao Ping; PENG Xiao Yun

doi:10.3967/bes2015.089

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Volume 28 Issue 9

Sep. 2015

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Article Navigation > Biomedical and Environmental Sciences > 2015 > 28(9): 634-641

ZHAO Xin Min, XIA Li Qiu, YANG Xiao Ping, PENG Xiao Yun. Flexibility Analysis of Bacillus thuringiensis Cry1Aa[J]. Biomedical and Environmental Sciences, 2015, 28(9): 634-641. doi: 10.3967/bes2015.089

Citation:

ZHAO Xin Min, XIA Li Qiu, YANG Xiao Ping, PENG Xiao Yun. Flexibility Analysis of Bacillus thuringiensis Cry1Aa[J]. Biomedical and Environmental Sciences, 2015, 28(9): 634-641. doi: 10.3967/bes2015.089

Flexibility Analysis of Bacillus thuringiensis Cry1Aa

doi: 10.3967/bes2015.089

Department of Chemistry and Environmental Engineering, Hunan City University, Yiyang 413000, Hunan, China
Key Laboratory of Microbial Molecular Biology of Hunan Province, College of Life Science, Hunan Normal University, Changsha 410081, Hunan, China

Funds: This study was supported by grants from the National Natural Science Foundation of China(30670052)%863 Program of China(2006AA02Z187)

Abstract

Objective To investigate the flexibility and mobility of the Bacillus thuringiensis toxin Cry1Aa.
Methods The 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.
Results The 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.
Conclusion Although several flexible regions could be found in all the three domains, the most flexible regions were in the apical loops of domain II.
- Flexibility,
- Cry1Aa,
- Bacillus thuringiensis,
- Constraint Network Analysis,
- NMSim
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通讯作者: 陈斌, bchen63@163.com

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沈阳化工大学材料科学与工程学院沈阳 110142

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Flexibility Analysis of Bacillus thuringiensis Cry1Aa

doi: 10.3967/bes2015.089

Department of Chemistry and Environmental Engineering, Hunan City University, Yiyang 413000, Hunan, China

Key Laboratory of Microbial Molecular Biology of Hunan Province, College of Life Science, Hunan Normal University, Changsha 410081, Hunan, China

Funds: This study was supported by grants from the National Natural Science Foundation of China(30670052)%863 Program of China(2006AA02Z187)

Key words:

Abstract: Objective To investigate the flexibility and mobility of the Bacillus thuringiensis toxin Cry1Aa.
Methods The 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.
Results The 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.
Conclusion Although several flexible regions could be found in all the three domains, the most flexible regions were in the apical loops of domain II.

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