1m0t

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(New page: 200px<br /><applet load="1m0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m0t, resolution 2.30&Aring;" /> '''Yeast Glutathione Sy...)
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[[Image:1m0t.jpg|left|200px]]<br /><applet load="1m0t" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m0t, resolution 2.30&Aring;" />
 
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'''Yeast Glutathione Synthase'''<br />
 
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==Overview==
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==Yeast Glutathione Synthase==
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Glutathione synthase catalyzes the final ATP-dependent step in glutathione, biosynthesis, the formation of glutathione from gamma-glutamylcysteine and, glycine. We have determined structures of yeast glutathione synthase in, two forms: unbound (2.3 A resolution) and bound to its substrate, gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions, (1.8 A resolution). These structures reveal that upon substrate binding, large domain motions convert the enzyme from an open unliganded form to a, closed conformation in which protein domains completely surround the, substrate in the active site.
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<StructureSection load='1m0t' size='340' side='right'caption='[[1m0t]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m0t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M0T 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]] 2.3&#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=SO4:SULFATE+ION'>SO4</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=1m0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0t OCA], [https://pdbe.org/1m0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m0t RCSB], [https://www.ebi.ac.uk/pdbsum/1m0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m0t ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1m0t TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSHB_YEAST GSHB_YEAST]
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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/m0/1m0t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1m0t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glutathione synthase catalyzes the final ATP-dependent step in glutathione biosynthesis, the formation of glutathione from gamma-glutamylcysteine and glycine. We have determined structures of yeast glutathione synthase in two forms: unbound (2.3 A resolution) and bound to its substrate gamma-glutamylcysteine, the ATP analog AMP-PNP, and two magnesium ions (1.8 A resolution). These structures reveal that upon substrate binding, large domain motions convert the enzyme from an open unliganded form to a closed conformation in which protein domains completely surround the substrate in the active site.
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==About this Structure==
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Large conformational changes in the catalytic cycle of glutathione synthase.,Gogos A, Shapiro L Structure. 2002 Dec;10(12):1669-76. PMID:12467574<ref>PMID:12467574</ref>
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1M0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M0T OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Large conformational changes in the catalytic cycle of glutathione synthase., Gogos A, Shapiro L, Structure. 2002 Dec;10(12):1669-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12467574 12467574]
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</div>
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[[Category: Glutathione synthase]]
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<div class="pdbe-citations 1m0t" style="background-color:#fffaf0;"></div>
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Burley, S.K.]]
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[[Category: Gogos, A.]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: Shapiro, L.]]
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[[Category: SO4]]
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[[Category: amine/carboxylate ligase]]
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[[Category: new york structural genomix research consortium]]
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[[Category: nysgxrc]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:02:53 2007''
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==See Also==
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*[[Glutathione synthetase|Glutathione synthetase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Burley SK]]
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[[Category: Gogos A]]
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[[Category: Shapiro L]]

Current revision

Yeast Glutathione Synthase

PDB ID 1m0t

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