Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA

By D. Mckay, T. Steitz. 1981

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Citations in the corpus

• PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis. (2005, background): “cNMP-binding occurs in a phosphate-binding cassette formed by the COOH-terminal -helices and the -barrel (375) (Fig.”
• The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors (2014, background): “Although CRP was the first transcriptional regulator whose three-dimensional structure was determined by crystallography [21], and a number of structures of the regulator bound to cAMP and DNA have been determined by crystallography [22–24], the Crystal Structures of GlxR from Corynebacterium glutam”
• Directed Evolution of the Escherichia coli cAMP Receptor Protein at the cAMP Pocket* (2015, background): “The crystal structures of the active CRP form have been reported several times since 1981 (7, 13, 14) (an active CRP structure complexed with bound DNA is shown in Fig.”
• Transcription activation by catabolite activator protein (CAP). (1999, background): “The crystallographic structure of CAP has been determined (McKay & Steitz, 1981), and several crystallographic structures of CAP in complex with DNA have been determined (Figure 1; Schultz et al., 1991; Parkinson et al. 1996a,b; Passner & Steitz, 1997; S. Chen, G. Parkinson, J. Liu, B. Benoff, H.…”
• Cyclic nucleotide-gated ion channels. (2002, background): “The three-dimensional structure of CAP has been determined by X-ray crystallography (265).”
• Origins of specificity in protein-DNA recognition (2010, unknown): “The first protein-DNA complexes for which structural information was derived from X-ray crystallography were the catabolite gene activator protein (CAP) (21), Cro repressor (22), and λ repressor (23) bound to their binding sites.”
• Catabolite activator protein: DNA binding and transcription activation. (2004, background): “DNA binding by CAP CAP is a dimer of two identical subunits, each of which is 209 residues in length and contains a helix-turn-helix DNA-binding motif [10].”
• Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. (2003, background): “CrpEc was the ¢rst transcription activator to be puri¢ed [27,28] and to have its X-ray structure revealed [29].”
• Handbook of ion channels (2015, background): “Although to date the crystal structure for a mammalian CNG channel CNBD has not been solved, the structures of many homologous CNBDs have been determined by x-ray crystallography or NMR (McKay and Steitz, 1981; Su et al., 1995; Zagotta et al., 2003; Clayton et al., 2004; Flynn et al., 2007; Das et a”
• Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, background): “CAP was the first transcription regulatory protein to have its 3D structure determined (5).”