7tec: Difference between revisions
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New page: '''Unreleased structure''' The entry 7tec is ON HOLD Authors: Schumacher, M.A. Description: Structure of the Listeria monocytogenes GlnR-DNA complex to 3.45 Angtrom [[Category: Unrelea... |
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==Structure of the Listeria monocytogenes GlnR-DNA complex to 3.45 Angstrom== | |||
<StructureSection load='7tec' size='340' side='right'caption='[[7tec]], [[Resolution|resolution]] 3.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7tec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] 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=7TEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TEC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.45Å</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=7tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tec OCA], [https://pdbe.org/7tec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tec RCSB], [https://www.ebi.ac.uk/pdbsum/7tec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tec ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/L8DSZ4_LISMN L8DSZ4_LISMN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
How bacteria sense and respond to nitrogen levels are central questions in microbial physiology. In Gram-positive bacteria, nitrogen homeostasis is controlled by an operon encoding glutamine synthetase (GS), a dodecameric machine that assimilates ammonium into glutamine, and the GlnR repressor. GlnR detects nitrogen excess indirectly by binding glutamine-feedback-inhibited-GS (FBI-GS), which activates its transcription-repression function. The molecular mechanisms behind this regulatory circuitry, however, are unknown. Here we describe biochemical and structural analyses of GS and FBI-GS-GlnR complexes from pathogenic and non-pathogenic Gram-positive bacteria. The structures show FBI-GS binds the GlnR C-terminal domain within its active-site cavity, juxtaposing two GlnR monomers to form a DNA-binding-competent GlnR dimer. The FBI-GS-GlnR interaction stabilizes the inactive GS conformation. Strikingly, this interaction also favors a remarkable dodecamer to tetradecamer transition in some GS, breaking the paradigm that all bacterial GS are dodecamers. These data thus unveil unique structural mechanisms of transcription and enzymatic regulation. | |||
Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.,Travis BA, Peck JV, Salinas R, Dopkins B, Lent N, Nguyen VD, Borgnia MJ, Brennan RG, Schumacher MA Nat Commun. 2022 Jul 1;13(1):3793. doi: 10.1038/s41467-022-31573-0. PMID:35778410<ref>PMID:35778410</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Schumacher | <div class="pdbe-citations 7tec" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Brennan RG]] | |||
[[Category: Schumacher MA]] | |||
Latest revision as of 17:03, 18 October 2023
Structure of the Listeria monocytogenes GlnR-DNA complex to 3.45 Angstrom
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