7tfe: Difference between revisions

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<StructureSection load='7tfe' size='340' side='right'caption='[[7tfe]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='7tfe' size='340' side='right'caption='[[7tfe]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7tfe]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFE FirstGlance]. <br>
<table><tr><td colspan='2'>[[7tfe]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7tfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfe OCA], [https://pdbe.org/7tfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfe RCSB], [https://www.ebi.ac.uk/pdbsum/7tfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfe 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=7tfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfe OCA], [https://pdbe.org/7tfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfe RCSB], [https://www.ebi.ac.uk/pdbsum/7tfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfe ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A5D5GA79_LISMN A0A5D5GA79_LISMN]
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>
==See Also==
 
*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tfe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutamate--ammonia ligase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peck, J]]
[[Category: Listeria monocytogenes]]
[[Category: Schumacher, M A]]
[[Category: Peck J]]
[[Category: Travis, B A]]
[[Category: Schumacher MA]]
[[Category: Biosynthetic protein]]
[[Category: Travis BA]]
[[Category: Glutamine synthetase dodecamer]]

Latest revision as of 13:08, 1 March 2024

L. monocytogenes GS(12) - apo

7tfe, resolution 2.85Å

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