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[[Image:1m0w.gif|left|200px]]
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{{STRUCTURE_1m0w|  PDB=1m0w  |  SCENE=  }}
'''Yeast Glutathione Synthase Bound to gamma-glutamyl-cysteine, AMP-PNP and 2 Magnesium Ions'''


==Yeast Glutathione Synthase Bound to gamma-glutamyl-cysteine, AMP-PNP and 2 Magnesium Ions==
<StructureSection load='1m0w' size='340' side='right'caption='[[1m0w]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m0w]] 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=1M0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M0W FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3GC:GAMMA-GLUTAMYLCYSTEINE'>3GC</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0w OCA], [https://pdbe.org/1m0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m0w RCSB], [https://www.ebi.ac.uk/pdbsum/1m0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m0w ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1m0w TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSHB_YEAST GSHB_YEAST]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m0/1m0w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1m0w ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1M0W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0W OCA].
</div>
<div class="pdbe-citations 1m0w" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Large conformational changes in the catalytic cycle of glutathione synthase., Gogos A, Shapiro L, Structure. 2002 Dec;10(12):1669-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12467574 12467574]
*[[Glutathione synthetase|Glutathione synthetase]]
[[Category: Glutathione synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Burley SK]]
[[Category: Burley, S K.]]
[[Category: Gogos A]]
[[Category: Gogos, A.]]
[[Category: Shapiro L]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Shapiro, L.]]
[[Category: Amine/carboxylate ligase]]
[[Category: New york structural genomix research consortium]]
[[Category: Nysgxrc]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:29:51 2008''

Latest revision as of 03:45, 6 June 2025

Yeast Glutathione Synthase Bound to gamma-glutamyl-cysteine, AMP-PNP and 2 Magnesium Ions

1m0w, resolution 1.80Å

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