Structural highlights
Publication Abstract from PubMed
Two-component systems are major signal transduction pathways, which consist of histidine kinases and response regulators that communicate through phosphorylation. Here, we highlight a distinct class of single-domain response regulators containing the PFXFATG[G/Y] motif that are activated by a mechanism distinct from the Y-T coupling described for prototypical receiver domains. We first solved the structures of inactive and active SdrG, a representative of the FAT GUY family, and then biochemically and genetically characterized variants in which residues in this motif were mutated. Our results support a model of activation mainly driven by a conserved lysine and reveal that the rotation of the threonine induces the reorganization of several aromatic residues in and around the PFXFATG[G/Y] motif to generate intermediates resembling those occurring during classical Y-T coupling. Overall, this helps define a new subfamily of response regulators that emerge as important players in physiological adaptation.
Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response.,Campagne S, Dintner S, Gottschlich L, Thibault M, Bortfeld-Miller M, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA Structure. 2016 Aug 2;24(8):1237-47. doi: 10.1016/j.str.2016.05.015. Epub 2016, Jul 7. PMID:27396826[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Campagne S, Dintner S, Gottschlich L, Thibault M, Bortfeld-Miller M, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA. Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response. Structure. 2016 Aug 2;24(8):1237-47. doi: 10.1016/j.str.2016.05.015. Epub 2016, Jul 7. PMID:27396826 doi:http://dx.doi.org/10.1016/j.str.2016.05.015
