Structural basis for cAMP-mediated allosteric control of the catabolite activator protein

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Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, background): “coli CAP, where the active conformation is achieved by a 60° rotation of a8 (46, 54, 55).”
The Transcriptional Regulators of the CRP Family Regulate Different Essential Bacterial Functions and Can Be Inherited Vertically and Horizontally (2017, background): “The crystal structure of the 45 KDa CRP-protein has been determined to a 2.1 Å resolution (Passner et al., 2000; Berrera et al., 2007); it consists of a dimer that suffers an allosteric transition when binding cAMP (Popovych et al., 2009).”
Directed Evolution of the Escherichia coli cAMP Receptor Protein at the cAMP Pocket* (2015, background): “However, the structures of the inactive CRP form have been solved only recently, using both crystallography and NMR spectroscopy (5, 6).”
Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, background): “Despite apparent conflicts with the reported NMR structure of apo CRP (Popovych et al., 2009), we conclude that the CDD dimerization of apo CRP would also be relevant in solution (see Supporting Information).”
Neglected role of cAMP receptor protein monomer (2011, background): “CRP monomers forms dimerization interface through C-helices and according to recent NMR structure T127 plays a key role in allosteric activation [23].”