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

Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.

The EMBO journal - 16 Jul 2001

van Tilbeurgh H, Le Coq D, Declerck N

Abstract excerpt

The transcriptional antiterminator protein LicT regulates the expression of Bacillus subtilis operons involved in beta-glucoside metabolism. It belongs to a newly characterized family of bacterial regulators whose activity is controlled by the phosphoenolpyruvate:sugar phosphotransferase system (PTS). LicT contains an N-terminal RNA-binding domain (56 residues), and a PTS regulation domain (PRD, 221 residues)...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Bacillus subtilis
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Dimerization

Share to Models, Molecular

Share to Phosphorylation

Share to Protein Conformation

Share to Sequence Homology, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 11447120
DOI: 10.1093/emboj/20.14.3789
PMCID: PMC125546

Genes

PTS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator.PMID 11447120Read ↗

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

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

Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon.Semantic proximity Read ↗

Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system.Semantic proximity Read ↗

Regulation of the Escherichia coli antiterminator protein BglG by phosphorylation at multiple sites and evidence for transfer of phosphoryl groups between monomers.Semantic proximity Read ↗

Opposing effects of histidine phosphorylation regulate the AtxA virulence transcription factor in Bacillus anthracis.Semantic proximity Read ↗

Crystal structure of Bacillus anthracis virulence regulator AtxA and effects of phosphorylated histidines on multimerization and activity.Semantic proximity Read ↗

Transcriptional control by two interacting regulatory proteins: identification of the PtxS binding site at PtxR.Semantic proximity Read ↗

Engineering an allosteric transcription factor to respond to new ligands.Semantic proximity Read ↗

An Adaptive Mutation in Enterococcus faecium LiaR Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes LiaR in an Activated State.Semantic proximity Read ↗

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