Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Proceedings of the National Academy of Sciences of the United States of America - 28 Apr 2009

Popovych Nataliya, Tzeng Shiou-Ru, Tonelli Marco, Ebright Richard H, Kalodimos Charalampos G

Abstract excerpt

The cAMP-mediated allosteric transition in the catabolite activator protein (CAP; also known as the cAMP receptor protein, CRP) is a textbook example of modulation of DNA-binding activity by small-molecule binding. Here we report the structure of CAP in the absence of cAMP, which, together with s...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Regulation
Share to Apoproteins
Share to Cyclic AMP

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP Receptor Protein

Share to Cyclic GMP

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 19359484
DOI: 10.1073/pnas.0900595106
PMCID: PMC2678429

Genes

CRP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19359484-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.PMID 19359484Read ↗

Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution.Semantic proximity Read ↗

Allosteric regulation of the cAMP receptor protein.Semantic proximity Read ↗

The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein.Semantic proximity Read ↗

The 1.6Å resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer.Semantic proximity Read ↗

Dissection of a surface-exposed portion of the cAMP-CRP complex that mediates transcription activation and repression.Semantic proximity Read ↗

Characteristics of the cAMP response unit.Semantic proximity Read ↗

Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains.Semantic proximity Read ↗

Structural Insights into of the Allosteric Activation of the LicT Antiterminator by PTS-Mediated Phosphorylation.Semantic proximity Read ↗

Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities.Semantic proximity Read ↗

Kinetic studies of cAMP-induced allosteric changes in mutants T127I, S128A, and T127I/S128A of the cAMP receptor protein from Escherichia coli.Semantic proximity Read ↗

CAP interacts with RNA polymerase in solution in the absence of promoter DNA.Semantic proximity Read ↗

Switching of the folding-energy landscape governs the allosteric activation of protein kinase A.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.