1lgr

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[[Image:1lgr.jpg|left|200px]]
 
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{{Structure
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==INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM==
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|PDB= 1lgr |SIZE=350|CAPTION= <scene name='initialview01'>1lgr</scene>, resolution 2.79&Aring;
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<StructureSection load='1lgr' size='340' side='right'caption='[[1lgr]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
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<table><tr><td colspan='2'>[[1lgr]] 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=1LGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LGR FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.79&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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}}
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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=1lgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lgr OCA], [https://pdbe.org/1lgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lgr RCSB], [https://www.ebi.ac.uk/pdbsum/1lgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lgr 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/1lgr_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=1lgr ConSurf].
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<div style="clear:both"></div>
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'''INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM'''
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==See Also==
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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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==Overview==
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== References ==
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Glutamine synthetase (GS) catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia in the presence of divalent cations. To gain insight into the structural basis of the feedback inhibition of GS by AMP, we have studied crystal structures of GS complexes with AMP and the related molecules: AMPPNP (a less hydrolyzable ATP analog), ADP, GDP, adenosine, and adenine. AMP is a feedback inhibitor of GS; ATP and ADP are cofactors, and AMPPNP, GDP, adenosine, and adenine are also GS inhibitors. GS used in this study is from Salmonella typhimurium and is free of covalent modification by adenylylation. All of the crystals examined contain two bound MN2+ ions per GS subunit. The X-ray structures show that all nucleotides bind at the same site, the cofactor ATP binding site, as do adenosine and adenine. Thus from X-ray structures, AMP, adenosine, adenine, and GDP would be expected to inhibit GS-Mn by competing with the substrate ATP for the active site. This suggestion from the crystal structures that AMP is competitive with respect to ATP is supported by kinetic measurements using the biosynthetic assay.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1LGR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LGR OCA].
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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==Reference==
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[[Category: Eisenberg D]]
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Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium., Liaw SH, Jun G, Eisenberg D, Biochemistry. 1994 Sep 20;33(37):11184-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7727369 7727369]
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[[Category: Liaw S-H]]
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[[Category: Glutamate--ammonia ligase]]
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[[Category: Salmonella typhimurium]]
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[[Category: Single protein]]
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[[Category: Eisenberg, D.]]
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[[Category: Liaw, S H.]]
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[[Category: AMP]]
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[[Category: MN]]
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[[Category: ligase(amide synthetase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:41 2008''
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Current revision

INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM

PDB ID 1lgr

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