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Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response.
- Source :
-
Structure (London, England : 1993) [Structure] 2016 Aug 02; Vol. 24 (8), pp. 1237-1247. Date of Electronic Publication: 2016 Jul 07. - Publication Year :
- 2016
-
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.<br /> (Copyright © 2016 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Motifs
Bacterial Proteins genetics
Bacterial Proteins metabolism
Binding Sites
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Lysine metabolism
Models, Molecular
Mutation
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Sphingomonas metabolism
Thermodynamics
Threonine metabolism
Bacterial Proteins chemistry
Lysine chemistry
Sphingomonas chemistry
Stress, Physiological genetics
Threonine chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 24
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 27396826
- Full Text :
- https://doi.org/10.1016/j.str.2016.05.015