1f52

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[[Image:1f52.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP==
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|PDB= 1f52 |SIZE=350|CAPTION= <scene name='initialview01'>1f52</scene>, resolution 2.49&Aring;
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<StructureSection load='1f52' size='340' side='right'caption='[[1f52]], [[Resolution|resolution]] 2.49&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>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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<table><tr><td colspan='2'>[[1f52]] 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=1F52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F52 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]] 2.49&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=1f52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f52 OCA], [https://pdbe.org/1f52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f52 RCSB], [https://www.ebi.ac.uk/pdbsum/1f52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f52 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/f5/1f52_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=1f52 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP'''
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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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==Overview==
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<references/>
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Phosphinothricin is a potent inhibitor of the enzyme glutamine synthetase (GS). The resolution of the native structure of GS from Salmonella typhimurium has been extended to 2.5 A resolution, and the improved model is used to determine the structure of phosphinothricin complexed to GS by difference Fourier methods. The structure suggests a noncovalent, dead-end mechanism of inhibition. Phosphinothricin occupies the glutamate substrate pocket and stabilizes the Glu327 flap in a position which blocks the glutamate entrance to the active site, trapping the inhibitor on the enzyme. One oxygen of the phosphinyl group of phosphinothricin appears to be protonated, because of its proximity to the carboxylate group of Glu327. The other phosphinyl oxygen protrudes into the negatively charged binding pocket for the substrate ammonium, disrupting that pocket. The distribution of charges in the glutamate binding pocket is complementary to those of phosphinothricin. The presence of a second ammonium binding site within the active site is confirmed by its analogue thallous ion, marking the ammonium site and its protein ligands. The inhibition of GS by methionine sulfoximine can be explained by the same mechanism. These models of inhibited GS further illuminate its catalytic mechanism.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1F52 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=1F52 OCA].
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Eisenberg D]]
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==Reference==
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[[Category: Gill HS]]
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The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition., Gill HS, Eisenberg D, Biochemistry. 2001 Feb 20;40(7):1903-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11329256 11329256]
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[[Category: Pfluegl GMU]]
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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: Gill, H S.]]
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[[Category: Pfluegl, G M.U.]]
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[[Category: ADP]]
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[[Category: MN]]
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[[Category: MPD]]
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[[Category: adp]]
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[[Category: glutamine synthetase]]
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[[Category: mpd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:44:30 2008''
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Current revision

CRYSTAL STRUCTURE OF GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM CO-CRYSTALLIZED WITH ADP

PDB ID 1f52

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