5IEB

Solution structure of SdrG from Sphingomonas melonis Fr1

Summary for 5IEB

• Entry DOI: 10.2210/pdb5ieb/pdb
• NMR Information: BMRB: 30023
• Descriptor: Sensory transduction regulatory protein (1 entity in total)
• Functional Keywords: single domain response regulator fat guy familly, protein
• Biological source: Sphingomonas melonis FR1
• Total number of polymer chains: 1
• Total formula weight: 13892.78

Authors

Campagne, S.,Vorholt, J.A.,Allain, F.H.-T. (deposition date: 2016-02-25, release date: 2016-07-20, Last modification date: 2024-05-15)

Primary citation

Campagne, S.,Dintner, S.,Gottschlich, L.,Thibault, M.,Bortfeld-Miller, M.,Kaczmarczyk, A.,Francez-Charlot, A.,Allain, F.H.,Vorholt, J.A.
Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response.
Structure, 24:1237-1247, 2016

PubMed Abstract: 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.

PubMed: 27396826
DOI: 10.1016/j.str.2016.05.015

Experimental method

SOLUTION NMR