5ieb: Difference between revisions
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==Solution structure of SdrG from Sphingomonas melonis Fr1== | |||
<StructureSection load='5ieb' size='340' side='right'caption='[[5ieb]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ieb]] 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=5IEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IEB FirstGlance]. <br> | |||
</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'>[https://proteopedia.org/fgij/fg.htm?mol=5ieb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ieb OCA], [https://pdbe.org/5ieb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ieb RCSB], [https://www.ebi.ac.uk/pdbsum/5ieb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ieb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0D1MA58_9SPHN A0A0D1MA58_9SPHN] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:27396826</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ieb" style="background-color:#fffaf0;"></div> | ||
[[Category: Allain | == References == | ||
[[Category: Campagne | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sphingomonas melonis FR1]] | |||
[[Category: Allain FH-T]] | |||
[[Category: Campagne S]] | |||
[[Category: Vorholt JA]] | |||
Latest revision as of 13:47, 30 August 2023
Solution structure of SdrG from Sphingomonas melonis Fr1
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