2n9u
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n9u]] is a 1 chain structure. 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> | ||
| + | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:27524295</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2n9u" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Correa, F]] | [[Category: Correa, F]] | ||
| - | [[Category: Gardner, K | + | [[Category: Gardner, K H]] |
| + | [[Category: Receiver]] | ||
| + | [[Category: Response regulator]] | ||
| + | [[Category: Transcription]] | ||
| + | [[Category: Two-component signaling]] | ||
Revision as of 20:59, 10 September 2016
Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain
| |||||||||||
