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| | ==Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain== | | ==Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain== |
| - | <StructureSection load='2n9u' size='340' side='right' caption='[[2n9u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2n9u' size='340' side='right'caption='[[2n9u]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n9u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Erylh Erylh]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N9U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter_litoralis_HTCC2594 Erythrobacter litoralis HTCC2594]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N9U FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ELI_10215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=314225 ERYLH])</td></tr> | + | </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=2n9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9u OCA], [https://pdbe.org/2n9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n9u RCSB], [https://www.ebi.ac.uk/pdbsum/2n9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9u ProSAT]</span></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=2n9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n9u OCA], [http://pdbe.org/2n9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n9u RCSB], [http://www.ebi.ac.uk/pdbsum/2n9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n9u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2N856_ERYLH Q2N856_ERYLH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Erylh]] | + | [[Category: Erythrobacter litoralis HTCC2594]] |
| - | [[Category: Correa, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Gardner, K H]] | + | [[Category: Correa F]] |
| - | [[Category: Receiver]] | + | [[Category: Gardner KH]] |
| - | [[Category: Response regulator]]
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| - | [[Category: Transcription]]
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| - | [[Category: Two-component signaling]]
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| Structural highlights
Function
Q2N856_ERYLH
Publication Abstract from PubMed
Information transmission in biological signaling networks is commonly considered to be a unidirectional flow of information between protein partners. According to this view, many bacterial response regulator proteins utilize input receiver (REC) domains to "switch" functional outputs, using REC phosphorylation to shift pre-existing equilibria between inactive and active conformations. However, recent data indicate that output domains themselves also shift such equilibria, implying a "mutual inhibition" model. Here we use solution nuclear magnetic resonance to provide a mechanistic basis for such control in a PhyR-type response regulator. Our structure of the isolated, non-phosphorylated REC domain surprisingly reveals a fully active conformation, letting us identify structural and dynamic changes imparted by the output domain to inactivate the full-length protein. Additional data reveal transient structural changes within the full-length protein, facilitating activation. Our data provide a basis for understanding the changes that REC and output domains undergo to set a default "inactive" state.
Basis of Mutual Domain Inhibition in a Bacterial Response Regulator.,Correa F, Gardner KH Cell Chem Biol. 2016 Aug 9. pii: S2451-9456(16)30240-9. doi:, 10.1016/j.chembiol.2016.07.010. PMID:27524295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Correa F, Gardner KH. Basis of Mutual Domain Inhibition in a Bacterial Response Regulator. Cell Chem Biol. 2016 Aug 9. pii: S2451-9456(16)30240-9. doi:, 10.1016/j.chembiol.2016.07.010. PMID:27524295 doi:http://dx.doi.org/10.1016/j.chembiol.2016.07.010
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