4r25: Difference between revisions

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'''Unreleased structure'''
==Structure of B. subtilis GlnK==
<StructureSection load='4r25' size='340' side='right' caption='[[4r25]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4r25]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R25 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r22|4r22]], [[4r24|4r24]]</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=4r25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r25 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r25 RCSB], [http://www.ebi.ac.uk/pdbsum/4r25 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NRGB_BACSU NRGB_BACSU]] Required for full induction of the nrgAB operon under conditions of ammonium limitation.<ref>PMID:14600241</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


The entry 4r25 is ON HOLD  until Paper Publication
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>


Authors: Schumacher, M.A.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Structure of B. subtilis GlnK
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Schumacher, M.A]]
__TOC__
</StructureSection>
[[Category: Schumacher, M A]]
[[Category: Nitrogen regulation]]
[[Category: Pii family member]]
[[Category: Tnra]]
[[Category: Transcription]]
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