title: Structural insights into the regulation of bacterial signalling proteins containing PRDs.
abstract: PRD-containing proteins are bacterial transcriptional antiterminators and activators characterised by a duplicated phosphorylation domain involved in the regulation of catabolic operons. Recent genetic and biochemical studies have suggested how the activity of these regulators is positively or negatively controlled through the multiple phosphorylation of conserved histidyl residues. The regulation mode of these proteins has been examined in light of the recently determined first crystal structure of the phosphorylatable domain of the LicT antiterminator.
authors.affiliation: Architecture et Fonction des Macromolécules Biologique, UMR 6098 du CNRS, Université d'Aix-Marseille, I et II, ESIL-GBMA, 163 Avenue de Luminy Case 925, 13288 Cedex 9, Marseille, France. herman@lebs.cnrs-gif.fr
authors.forename: H
authors.initials: H
authors.lastname: van Tilbeurgh
authors.forename: N
authors.initials: N
authors.lastname: Declerck
mesh_terms: D001426:Bacterial Proteins / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D014158:Transcription, Genetic
chemical_list: D001426:Bacterial Proteins