2lgs

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(New page: 200px<br /><applet load="2lgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="2lgs, resolution 2.8&Aring;" /> '''FEEDBACK INHIBITION O...)
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[[Image:2lgs.jpg|left|200px]]<br /><applet load="2lgs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2lgs, resolution 2.8&Aring;" />
 
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'''FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE'''<br />
 
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==Overview==
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==FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE==
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Bacterial glutamine synthetase (GS; EC 6.3.1.2) was previously shown to be, inhibited by nine end products of glutamine metabolism. Here we present, four crystal structures of GS, complexed with the substrate Glu and with, each of three feedback inhibitors. The GS of the present study is from, Salmonella typhimurium, with Mn2+ ions bound, and is fully unadenylylated., From Fourier difference maps, we find that L-serine, L-alanine, and, glycine bind at the site of the substrate L-glutamate. In our model, these, four amino acids bind with the atoms they share in common (the "main, chain" +NH3-CH-COO-) in the same positions. Thus on the basis of our x-ray, work, glycine, alanine, and serine appear to inhibit GS-Mn by competing, with the substrate glutamate for the active site.
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<StructureSection load='2lgs' size='340' side='right'caption='[[2lgs]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2lgs]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LGS 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]] 2.8&#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=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=2lgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgs OCA], [https://pdbe.org/2lgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgs RCSB], [https://www.ebi.ac.uk/pdbsum/2lgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLN1B_SALTY GLN1B_SALTY] Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.<ref>PMID:7727369</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lg/2lgs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2lgs ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2LGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with MN and GLU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2LGS OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
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==Reference==
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== References ==
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Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine., Liaw SH, Pan C, Eisenberg D, Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4996-5000. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8099447 8099447]
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<references/>
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[[Category: Glutamate--ammonia ligase]]
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__TOC__
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[[Category: Salmonella typhimurium]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Eisenberg, D.]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Liaw, S.H.]]
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[[Category: Eisenberg D]]
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[[Category: GLU]]
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[[Category: Liaw S-H]]
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[[Category: MN]]
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[[Category: ligase(amide synthetase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:41:59 2007''
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Current revision

FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE

PDB ID 2lgs

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