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7tfa

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Current revision (13:08, 1 March 2024) (edit) (undo)
 
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<StructureSection load='7tfa' size='340' side='right'caption='[[7tfa]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
<StructureSection load='7tfa' size='340' side='right'caption='[[7tfa]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7tfa]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7tfa]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_polymyxa Paenibacillus polymyxa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.07&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <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=7tfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfa OCA], [https://pdbe.org/7tfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfa RCSB], [https://www.ebi.ac.uk/pdbsum/7tfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfa 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=7tfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfa OCA], [https://pdbe.org/7tfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfa RCSB], [https://www.ebi.ac.uk/pdbsum/7tfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfa ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0F0G8G2_PAEPO A0A0F0G8G2_PAEPO]
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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.
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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>
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==See Also==
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*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7tfa" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamate--ammonia ligase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peck, J]]
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[[Category: Paenibacillus polymyxa]]
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[[Category: Schumacher, M A]]
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[[Category: Peck J]]
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[[Category: Travis, B A]]
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[[Category: Schumacher MA]]
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[[Category: Biosynthetic protein]]
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[[Category: Travis BA]]
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[[Category: Glutamine synthetase repressor dodecamer]]
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[[Category: Ligase]]
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Current revision

P. polymyxa GS(12)-Q-GlnR peptide

PDB ID 7tfa

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OCA

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