Article
Kinetic studies of cAMP-induced allosteric changes in mutants T127I, S128A, and T127I/S128A of the cAMP receptor protein from Escherichia coli.
The Journal of biological chemistry - 31 Oct 2003
Polit Agnieszka, Bonarek Piotr, Kepys Barbara, Kedracka-Krok Sylwia, Górecki Andrzej, Wasylewski Zygmunt
Abstract excerpt
The cAMP receptor protein (CRP) regulates the expression of several genes in Escherichia coli. The protein is a homodimer, and each monomer is folded into two distinct structural domains. After allosteric transitions resulting from the binding of cAMP, CRP specifically binds to DNA and activates transcription. We have used stopped-flow fluorometry measurements of CRP mutants bearing amino acid substitutions...
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