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| | <StructureSection load='4r4e' size='340' side='right'caption='[[4r4e]], [[Resolution|resolution]] 2.57Å' scene=''> | | <StructureSection load='4r4e' size='340' side='right'caption='[[4r4e]], [[Resolution|resolution]] 2.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R4E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r4e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R4E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glnR, BSU17450 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene></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=4r4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r4e OCA], [http://pdbe.org/4r4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r4e RCSB], [http://www.ebi.ac.uk/pdbsum/4r4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r4e 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=4r4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r4e OCA], [https://pdbe.org/4r4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r4e RCSB], [https://www.ebi.ac.uk/pdbsum/4r4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r4e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLNR_BACSU GLNR_BACSU]] Represses many genes including the glnRA operon and tnrA during growth with nitrogen excess.<ref>PMID:10231480</ref> <ref>PMID:1677938</ref> <ref>PMID:2573733</ref> | + | [https://www.uniprot.org/uniprot/GLNR_BACSU GLNR_BACSU] Represses many genes including the glnRA operon and tnrA during growth with nitrogen excess.<ref>PMID:10231480</ref> <ref>PMID:1677938</ref> <ref>PMID:2573733</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | All cells must sense and adapt to changing nutrient availability. However, detailed molecular mechanisms coordinating such regulatory pathways remain poorly understood. In Bacillus subtilis, nitrogen homeostasis is controlled by a unique circuitry composed of the regulator TnrA, which is deactivated by feedback-inhibited glutamine synthetase (GS) during nitrogen excess and stabilized by GlnK upon nitrogen depletion, and the repressor GlnR. Here we describe a complete molecular dissection of this network. TnrA and GlnR, the global nitrogen homeostatic transcription regulators, are revealed as founders of a new structural family of dimeric DNA-binding proteins with C-terminal, flexible, effector-binding sensors that modulate their dimerization. Remarkably, the TnrA sensor domains insert into GS intersubunit catalytic pores, destabilizing the TnrA dimer and causing an unprecedented GS dodecamer-to-tetradecamer conversion, which concomitantly deactivates GS. In contrast, each subunit of the GlnK trimer "templates" active TnrA dimers. Unlike TnrA, GlnR sensors mediate an autoinhibitory dimer-destabilizing interaction alleviated by GS, which acts as a GlnR chaperone. Thus, these studies unveil heretofore unseen mechanisms by which inducible sensor domains drive metabolic reprograming in the model Gram-positive bacterium B. subtilis.
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| - | Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis.,Schumacher MA, Chinnam NB, Cuthbert B, Tonthat NK, Whitfill T Genes Dev. 2015 Feb 15;29(4):451-64. doi: 10.1101/gad.254714.114. PMID:25691471<ref>PMID:25691471</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4r4e" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schumacher, M A]] | + | [[Category: Synthetic construct]] |
| - | [[Category: B. subtili]] | + | [[Category: Schumacher MA]] |
| - | [[Category: Dna]]
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| - | [[Category: Gs-q]]
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| - | [[Category: New member]]
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| - | [[Category: Nitrogen homeostasis]]
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| - | [[Category: Nucleoid]]
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| - | [[Category: Tnra/glnr dna-binding family of winged-hth with c-terminal inducer/sensor domain]]
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| - | [[Category: Tnra/glnr family]]
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| - | [[Category: Transcription]]
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| - | [[Category: Transcription regulator-dna complex]]
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