7tf6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==S. aureus GS(12)-Q-GlnR peptide== | |
| + | <StructureSection load='7tf6' size='340' side='right'caption='[[7tf6]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7tf6]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TF6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.15Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7tf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tf6 OCA], [https://pdbe.org/7tf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tf6 RCSB], [https://www.ebi.ac.uk/pdbsum/7tf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tf6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/E3VXC2_STAAU E3VXC2_STAAU] Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.[ARBA:ARBA00002161] | ||
| - | + | ==See Also== | |
| - | + | *[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Staphylococcus aureus]] | ||
| + | [[Category: Peck J]] | ||
| + | [[Category: Schumacher MA]] | ||
| + | [[Category: Travis BA]] | ||
Current revision
S. aureus GS(12)-Q-GlnR peptide
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