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PDBsum entry 5ieb
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DOI no:
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Structure
24:1237-1247
(2016)
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PubMed id:
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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.
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S.Campagne,
S.Dintner,
L.Gottschlich,
M.Thibault,
M.Bortfeld-Miller,
A.Kaczmarczyk,
A.Francez-Charlot,
F.H.Allain,
J.A.Vorholt.
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ABSTRACT
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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.
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');
}
}
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