3wd6
From Proteopedia
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| - | ''' | + | ==Crystal structure of Bombyx mori omega-class glutathione transferase in complex with GSH== |
| + | <StructureSection load='3wd6' size='340' side='right' caption='[[3wd6]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wd6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WD6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WD6 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene><br> | ||
| + | <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=3wd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wd6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wd6 RCSB], [http://www.ebi.ac.uk/pdbsum/3wd6 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glutathione transferases (GSTs) are major phase II detoxification enzymes that play central roles in the defense against various environmental toxicants as well as oxidative stress. Here we report the crystal structure of an Omega-class glutathione transferase of Bombyx mori, bmGSTO, to gain insight into its catalytic mechanism. The structure of bmGSTO complexed with glutathione determined at a resolution of 2.5A reveals that it exists as a dimer and is structurally similar to Omega-class GSTs with respect to its secondary and tertiary structures. Analysis of a complex between bmGSTO and glutathione showed that bound glutathione was localized to the glutathione-binding site (G-site). Site-directed mutagenesis of bmGSTO mutants indicated that amino acid residues Leu62, Lys65, Lys77, Val78, Glu91 and Ser92 in the G-site contribute to catalytic activity. | ||
| - | + | Three-dimensional structure of a Bombyx mori Omega-class glutathione transferase.,Yamamoto K, Suzuki M, Higashiura A, Nakagawa A Biochem Biophys Res Commun. 2013 Sep 6;438(4):588-93. doi:, 10.1016/j.bbrc.2013.08.011. Epub 2013 Aug 11. PMID:23939046<ref>PMID:23939046</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Higashiura, A.]] | ||
| + | [[Category: Nakagawa, A.]] | ||
| + | [[Category: Suzuki, M.]] | ||
| + | [[Category: Yamamoto, K.]] | ||
| + | [[Category: Electron sharing network]] | ||
| + | [[Category: Glutathione binding]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:19, 16 July 2014
Crystal structure of Bombyx mori omega-class glutathione transferase in complex with GSH
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