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

Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.

The Journal of biological chemistry - 15 Apr 2005

Graille Marc, Zhou Cong-Zhao, Receveur-Bréchot Véronique, Collinet Bruno, Declerck Nathalie, van Tilbeurgh Herman

Abstract excerpt

The transcriptional antiterminator protein LicT regulates the expression of Bacillus subtilis operons involved in beta-glucoside metabolism. It consists of an N-terminal RNA-binding domain (co-antiterminator (CAT)) and two phosphorylatable phosphotransferase system regulation domains (PRD1 and PRD2). In the activated state, each PRD forms a dimeric unit with the phosphorylation sites totally buried at the dimer...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Protein Conformation

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Share to Scattering, Radiation

Share to X-Rays

Source

Identifiers

PMID: 15699035
DOI: 10.1074/jbc.M414642200

Genes

CAT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.PMID 15699035Read ↗

Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.Semantic proximity Read ↗

Dimer stabilization upon activation of the transcriptional antiterminator LicT.Semantic proximity Read ↗

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

Mycobacterium tuberculosis CarD, an essential global transcriptional regulator forms amyloid-like fibrils.Semantic proximity Read ↗

Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases.Semantic proximity Read ↗

Evolution of oligomeric state through allosteric pathways that mimic ligand binding.Semantic proximity Read ↗

The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation.Semantic proximity Read ↗

Two-state allosteric behavior in a single-domain signaling protein.Semantic proximity Read ↗

Experimental and computational characterization of the dimerization of the PTS-regulation domains of BglG from Escherichia coli.Semantic proximity Read ↗

Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.Semantic proximity Read ↗

Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C.Semantic proximity Read ↗

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