Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution.

By I. Weber, T. Steitz. 1987

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Citations in the corpus

Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, background): “This is further supported by similar equilibrium shifts that have been introduced via mutations of E. coli CAP before (64). cAMP binding initiates the population shift by interacting with residues of the central helices of both subunits (CAP:T127 and CAP:S128) (65).”
Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface. (1997, background): “In both CAP subunits, the domain-domain interface is in a ‘‘closed’’ conformation (see Weber & Steitz, 1987), and the bound cAMP molecule exhibits an anti glycosidic-bond conformation (Figure 2(a),(b)).”
Nitrogen Control in Cyanobacteria (2001, background): “3), the former of which participates in protein dimerization (106) and contributes three residues (Arg(123), Thr(127), and Ser(128)) that contact cAMP (83, 123), the Arg and Thr residues being conserved in NtcA (Arg(128) and Thr(132), respectively, of strain PCC 7942 NtcA).”
The voltage-gated potassium channels and their relatives (2002, background): “The CNG channels use a C-terminal nucleotide-binding domain that is closely related to the dimeric catabolite activator protein of bacteri”
cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review (2008, methodology): “As far as secondary structure is concerned, it is known that this domain is formed by three helices (A, B, C) and eight strands, which are located in the antiparallel orientation to create a barrel where the first cAMP-binding site is situated [Weber and Steitz, 1987].”
Fourier transform infrared spectroscopic analysis of protein secondary structures. (2007, background): “There is a bias in the distribution of secondary structural elements between the two functional domains, namely extensive β-sheets in the cAMP binding domain and predominant α-helices in the DNA binding domain [ 42 ,43].”
Cyclic nucleotide-gated ion channels. (2002, background): “At the equivalent position in CAP, residue T127 in one subunit and S128 from the opposite subunit of the CAP dimer form hydrogen bonds with the N2C amino group of adenine (409) (Fig.”
Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, methodology): “Stepwise binding and specific recognition of syn cGMP Through a close inspection of the cAMP–CRP structure, Weber & Steitz (1987) supposed that cAMP first binds to the -roll residues via interactions with the phosphoribose, which is followed by adenine interactions.”