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4lni

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{{Large structure}}
 
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{{STRUCTURE_4lni| PDB=4lni | SCENE= }}
 
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===B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex===
 
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==About this Structure==
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==B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex==
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[[4lni]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNI OCA].
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<StructureSection load='4lni' size='340' side='right'caption='[[4lni]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4lni]] is a 12 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=4LNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LNI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5793&#8491;</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lni OCA], [https://pdbe.org/4lni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lni RCSB], [https://www.ebi.ac.uk/pdbsum/4lni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lni ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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==See Also==
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*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Glutamate--ammonia ligase]]
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[[Category: Large Structures]]
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[[Category: Chinnam, N.]]
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[[Category: Chinnam N]]
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[[Category: Fisher, S.]]
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[[Category: Fisher S]]
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[[Category: Schumacher, M A.]]
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[[Category: Schumacher MA]]
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[[Category: Tonthat, N.]]
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[[Category: Tonthat N]]
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[[Category: Wray, L.]]
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[[Category: Wray L]]
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[[Category: Alpha-beta]]
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[[Category: Glnra]]
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[[Category: Ligase]]
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[[Category: Tnra]]
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Current revision

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex

PDB ID 4lni

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