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==Complete dissection of B. subtilis nitrogen homeostatic circuitry==
==Complete dissection of B. subtilis nitrogen homeostatic circuitry==
<StructureSection load='4r24' size='340' side='right' caption='[[4r24]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='4r24' size='340' side='right'caption='[[4r24]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4r24]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R24 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4r24]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_WSH-002 Priestia megaterium WSH-002] 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=4R24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R24 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r22|4r22]], [[4r25|4r25]]</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]] 2.25&#8491;</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=4r24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r24 OCA], [http://pdbe.org/4r24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r24 RCSB], [http://www.ebi.ac.uk/pdbsum/4r24 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r24 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=4r24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r24 OCA], [https://pdbe.org/4r24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r24 RCSB], [https://www.ebi.ac.uk/pdbsum/4r24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r24 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/TNRA_PRIMW TNRA_PRIMW] Transcription regulator that actives the transcription of genes required for nitrogen assimilation during nitrogen limitation. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site.[UniProtKB:Q45666]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4r24" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Schumacher, M A]]
[[Category: Large Structures]]
[[Category: B. subtili]]
[[Category: Priestia megaterium WSH-002]]
[[Category: Glnk]]
[[Category: Synthetic construct]]
[[Category: G]]
[[Category: Schumacher MA]]
[[Category: New dna-binding family]]
[[Category: Nucleoid]]
[[Category: Tnra]]
[[Category: Transcription]]
[[Category: Transcrption-dna complex]]
[[Category: With winged hth]]
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