7ten: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the Listeria monocytogenes GS-Met-Sox-P- ADP complex to 3.5 Angstrom== | ==Crystal structure of the Listeria monocytogenes GS-Met-Sox-P- ADP complex to 3.5 Angstrom== | ||
<StructureSection load='7ten' size='340' side='right'caption='[[7ten]]' scene=''> | <StructureSection load='7ten' size='340' side='right'caption='[[7ten]], [[Resolution|resolution]] 3.50Å' 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=7TEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TEN FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ten]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TEN 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=7ten FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ten OCA], [https://pdbe.org/7ten PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ten RCSB], [https://www.ebi.ac.uk/pdbsum/7ten PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ten 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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</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=7ten FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ten OCA], [https://pdbe.org/7ten PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ten RCSB], [https://www.ebi.ac.uk/pdbsum/7ten PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ten ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<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 7ten" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glutamate--ammonia ligase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Schumacher, | [[Category: Schumacher, M A]] | ||
[[Category: Glnr]] | |||
[[Category: Glutamate ammonium ligase]] | |||
[[Category: Glutamine synthetase]] | |||
[[Category: Ligase]] | |||
[[Category: Ligase-inhibitor complex]] | |||
[[Category: Met-sox]] | |||
[[Category: Transition state]] | |||
Revision as of 05:12, 10 August 2022
Crystal structure of the Listeria monocytogenes GS-Met-Sox-P- ADP complex to 3.5 Angstrom
| ||||||||||||
