1m0t

<table><tr><td colspan='2'>[[1m0t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1M0T FirstGlance]. <br>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hgs|2hgs]], [[1m0w|1m0w]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0t OCA], [http://pdbe.org/1m0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m0t RCSB], [http://www.ebi.ac.uk/pdbsum/1m0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m0t ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1m0t TOPSAN]</span></td></tr>

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m0t" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Glutathione synthase]]

[[Category: Burley, S K]]

[[Category: Gogos, A]]

[[Category: Structural genomic]]

[[Category: Shapiro, L]]

[[Category: PSI, Protein structure initiative]]