Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein

The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upo...

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Bibliographic Details
Published in:International journal of biological macromolecules 2012-01, Vol.50 (1), p.1-6
Main Authors: Gao, Zhengya, Li, Feng, Wu, Guangrong, Zhu, Yanrun, Yu, Ting, Yu, Shaoning
Format: Article
Language:English
Subjects:
adenosine monophosphate
Amino Acid Motifs
Calorimetry - methods
cAMP
cAMP binding motif
cAMP receptor protein
Chymotrypsin - chemistry
Circular Dichroism
Conformational change
cyclic AMP
Cyclic AMP Receptor Protein - chemistry
Cyclic AMP Receptor Protein - metabolism
Dimerization
Escherichia coli
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
genes
Kinetics
Macromolecular Substances - chemistry
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Signal Transduction
Spectrometry, Fluorescence - methods
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Temperature
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Summary:The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2011.08.016