1m0t
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Yeast Glutathione Synthase== |
+ | <StructureSection load='1m0t' size='340' side='right' caption='[[1m0t]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1m0t]] is a 2 chain structure with 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=1M0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M0T FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hgs|2hgs]], [[1m0w|1m0w]]</td></tr> | ||
+ | <tr><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 Saccharomyces cerevisiae])</td></tr> | ||
+ | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m0t RCSB], [http://www.ebi.ac.uk/pdbsum/1m0t PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1m0t TOPSAN]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/m0/1m0t_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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. | ||
- | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Glutathione synthetase|Glutathione synthetase]] | *[[Glutathione synthetase|Glutathione synthetase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Glutathione synthase]] | [[Category: Glutathione synthase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] |
Revision as of 18:24, 28 September 2014
Yeast Glutathione Synthase
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Categories: Glutathione synthase | Saccharomyces cerevisiae | Burley, S K. | Gogos, A. | NYSGXRC, New York SGX Research Center for Structural Genomics. | Shapiro, L. | Amine/carboxylate ligase | Ligase | New york sgx research center for structural genomic | Nysgxrc | Protein structure initiative | Psi | Structural genomic