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7tfc
From Proteopedia
(Difference between revisions)
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| - | == | + | ==B. subtilis GS(14)-Q-GlnR peptide== |
| - | <StructureSection load='7tfc' size='340' side='right'caption='[[7tfc]]' scene=''> | + | <StructureSection load='7tfc' size='340' side='right'caption='[[7tfc]], [[Resolution|resolution]] 1.96Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7tfc]] is a 28 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TFC FirstGlance]. <br> |
| - | </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=7tfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfc OCA], [https://pdbe.org/7tfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfc RCSB], [https://www.ebi.ac.uk/pdbsum/7tfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfc ProSAT]</span></td></tr> | + | </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> |
| + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7tfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tfc OCA], [https://pdbe.org/7tfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tfc RCSB], [https://www.ebi.ac.uk/pdbsum/7tfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tfc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/GLNR_BACSU GLNR_BACSU]] Represses many genes including the glnRA operon and tnrA during growth with nitrogen excess.<ref>PMID:10231480</ref> <ref>PMID:1677938</ref> <ref>PMID:2573733</ref> | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7tfc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Glutamate--ammonia ligase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Peck, J]] |
| + | [[Category: Schumacher, M A]] | ||
| + | [[Category: Travis, B A]] | ||
| + | [[Category: Biosynthetic protein]] | ||
| + | [[Category: Glutamine synthetase repressor tetradecamer]] | ||
| + | [[Category: Ligase]] | ||
Revision as of 05:12, 10 August 2022
B. subtilis GS(14)-Q-GlnR peptide
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