Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface.

By G. Parkinson, Christopher Wilson, A. Gunasekera, Y. Ebright, Richard E. Ebright, Helen M. Berman. 1997

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Citations in the corpus

cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review (2008, methodology): “When CRP binds DNA, it makes the nucleic acid bend about 87° in the case of consensus sequence [Parkinson et al., 1996].”
Catabolite activator protein: DNA binding and transcription activation. (2004, background): “By contrast, sequence preferences at the remaining positions occur in the absence of amino acid–base contacts and thus must involve indirect readout (Figure 1b) [12,13].”
Transcription activation by catabolite activator protein (CAP). (1999, background): “For simplicity, DNA is drawn straight; in point of fact, both CAP and RNAP bend DNA (Schultz et al., 1991; Parkinson et al., 1996a,b; Rees et al., 1993; Meyer-Almes et al., 1994; Rivetti et al., 1999).”
DNA Deformation Energy as an Indirect Recognition Mechanism in Protein-DNA Interactions (2007, background): “All sequences known to bind to IHF [23], CRP [19], [20], I-CreI [21] , I-PpoI [21], and SRF [22] at high affinities were identified from the available literature (see supplemental data).”
Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, background): “The 3D structures of CAP have been determined in its cAMP-bound state (6) and in its cAMP-bound state in complex with DNA (7, 8).”
Three-dimensional EM structure of an intact activator-dependent transcription initiation complex (2009, background): “Structures of CAP-DNA complexes indicate that CAP bends its DNA site by 80° (5, 6).”