4lno: Difference between revisions

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 ==B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1==
-<StructureSection load='4lno' size='340' side='right' caption='[[4lno]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='4lno' size='340' side='right'caption='[[4lno]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4lno]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LNO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4lno]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LNO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lnf|4lnf]], [[4lni|4lni]], [[4lnk|4lnk]], [[4lnn|4lnn]]</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=4lno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lno OCA], [https://pdbe.org/4lno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lno RCSB], [https://www.ebi.ac.uk/pdbsum/4lno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lno ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glnA, BSU17460 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lno OCA], [http://pdbe.org/4lno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lno RCSB], [http://www.ebi.ac.uk/pdbsum/4lno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lno ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GLN1A_BACSU GLN1A_BACSU] 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 (PubMed:25691471). It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:24158439). Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA (PubMed:11719184, PubMed:12139611). During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation (PubMed:11719184, PubMed:12139611, PubMed:25691471). Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity (PubMed:11719184, PubMed:12139611, PubMed:25691471). 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 (PubMed:25691471).<ref>PMID:11719184</ref> <ref>PMID:12139611</ref> <ref>PMID:24158439</ref> <ref>PMID:25691471</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 18: @@
 </div>
 <div class="pdbe-citations 4lno" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Bacillus subtilis]]
-[[Category: Glutamate--ammonia ligase]]
+[[Category: Large Structures]]
-[[Category: Chinnam, N]]
+[[Category: Chinnam N]]
-[[Category: Fisher, S]]
+[[Category: Fisher S]]
-[[Category: Schumacher, M A]]
+[[Category: Schumacher MA]]
-[[Category: Tonthat, N]]
+[[Category: Tonthat N]]
-[[Category: Wray, L]]
+[[Category: Wray L]]
-[[Category: Alpha/beta]]
-[[Category: Glnr]]
-[[Category: Ligase]]
-[[Category: Tnra]]