5iej | pdb_00005iej

Solution structure of the BeF3-activated conformation of SdrG from Pseudomonas melonis Fr1

spinqualitylabelsall models 5iej Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5iej is a 1 chain structure with sequence from Sphingomonas melonis FR1. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1C7D1A8_9SPHN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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