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| | ==Solution structure of the BeF3-activated conformation of SdrG from Pseudomonas melonis Fr1== | | ==Solution structure of the BeF3-activated conformation of SdrG from Pseudomonas melonis Fr1== |
| - | <StructureSection load='5iej' size='340' side='right'caption='[[5iej]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5iej' size='340' side='right'caption='[[5iej]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iej]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphingomonas_melonis_fr1 Sphingomonas melonis fr1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IEJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_melonis_FR1 Sphingomonas melonis FR1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IEJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ieb|5ieb]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iej OCA], [http://pdbe.org/5iej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iej RCSB], [http://www.ebi.ac.uk/pdbsum/5iej PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iej ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iej OCA], [https://pdbe.org/5iej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iej RCSB], [https://www.ebi.ac.uk/pdbsum/5iej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iej ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1C7D1A8_9SPHN A0A1C7D1A8_9SPHN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sphingomonas melonis fr1]] | + | [[Category: Sphingomonas melonis FR1]] |
| - | [[Category: Allain, F H.T]] | + | [[Category: Allain FH-T]] |
| - | [[Category: Campagne, S]] | + | [[Category: Campagne S]] |
| - | [[Category: Vorholt, J A]] | + | [[Category: Vorholt JA]] |
| - | [[Category: Protein]]
| + | |
| - | [[Category: Single domain response regulator fat guy response regulator allosteric transition general stress response]]
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| Structural highlights
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[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
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