Proposed structural mechanism of Escherichia coli cAMP receptor protein cAMP-dependent proteolytic cleavage protection and selective and nonselective DNA binding.

By S. Scott, Shadi Jarjous. 2005

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Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “R180, E181 and R185 are the key residues of the HTH motif involved in specific protein-DNA interactions [6], whereas the nonspecific DNA binding residues are R169, Q170 and S179 [7] with the other DNA binding sites [8] D138, V139, T168, C178, T182, G184, K188, H199, and G200.”
Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, background): “…a challenge (Won et al., 2009; Tutar, 2008; Scott & Jarjous, 2005; Małecki et al., 2000) since the identification of additional cAMP-specific binding sites at the CDDs, which are formed after complete occupancy of the N-terminal cNMP-binding sites by cAMPs (Won et al., 2002; Scott & Jarjous, 2005).”
Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli (2008, background): “Finally, the possibility of the binding of ligands to the secondary cAMP-binding site in CRP is highly unlikely to be relevant to the present study, based on the previously reported requirement for much higher ligand concentrations for binding there (24, 34).”