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| | <StructureSection load='3mak' size='340' side='right'caption='[[3mak]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3mak' size='340' side='right'caption='[[3mak]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MAK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3f6f|3f6f]], [[3gh6|3gh6]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></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=3mak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mak OCA], [https://pdbe.org/3mak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mak RCSB], [https://www.ebi.ac.uk/pdbsum/3mak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mak ProSAT]</span></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=3mak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mak OCA], [https://pdbe.org/3mak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mak RCSB], [https://www.ebi.ac.uk/pdbsum/3mak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mak ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GSTT1_DROME GSTT1_DROME]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.
| + | [https://www.uniprot.org/uniprot/GSTD1_DROME GSTD1_DROME] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028, PubMed:20417639). Has DDT dehydrochlorinase activity (PubMed:20417639). May be involved in detoxification (PubMed:22082028).<ref>PMID:20417639</ref> <ref>PMID:22082028</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Glutathione transferase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ketterman, A J]] | + | [[Category: Ketterman AJ]] |
| - | [[Category: Robinson, R C]] | + | [[Category: Robinson RC]] |
| - | [[Category: Wongsantichon, J]] | + | [[Category: Wongsantichon J]] |
| - | [[Category: Protein-substrate complex]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GSTD1_DROME Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028, PubMed:20417639). Has DDT dehydrochlorinase activity (PubMed:20417639). May be involved in detoxification (PubMed:22082028).[1] [2]
Publication Abstract from PubMed
We report four new crystal structures for Delta class glutathione transferases from insects. We compare these new structures as well as several previously reported structures to determine that structural transitions can be observed with ligand binding. These transitions occurred in the regions around the active site entrance, including alpha helix 2, C-terminus of alpha helix 4 including the loop to helix 5 and the C-terminus of helix 8. These structural movements have been reported or postulated to occur for several other glutathione transferase classes; however, this is the first report showing structural evidence of all these movements occurring, in this case in Delta class glutathione transferases. These fluctuations also can be observed occurring within a single structure as there is ligand bound in only one subunit and each subunit is undergoing different conformational transitions. The structural comparisons show reorganizations occur both pre- and post-GSH ligand binding communicated through the subunit interface of the quaternary assembly. Movements of these positions would allow 'breathing' of the active site for substrate entrance, topological rearrangement for varying substrate specificity and final product release.
Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding.,Wongsantichon J, Robinson RC, Ketterman AJ Arch Biochem Biophys. 2012 May;521(1-2):77-83. doi: 10.1016/j.abb.2012.03.023., Epub 2012 Mar 27. PMID:22475449[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Low WY, Feil SC, Ng HL, Gorman MA, Morton CJ, Pyke J, McConville MJ, Bieri M, Mok YF, Robin C, Gooley PR, Parker MW, Batterham P. Recognition and detoxification of the insecticide DDT by Drosophila melanogaster glutathione S-transferase D1. J Mol Biol. 2010 Jun 11;399(3):358-66. Epub 2010 Apr 24. PMID:20417639 doi:10.1016/j.jmb.2010.04.020
- ↑ Saisawang C, Wongsantichon J, Ketterman AJ. A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster. Biochem J. 2012 Feb 15;442(1):181-90. doi: 10.1042/BJ20111747. PMID:22082028 doi:http://dx.doi.org/10.1042/BJ20111747
- ↑ Wongsantichon J, Robinson RC, Ketterman AJ. Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding. Arch Biochem Biophys. 2012 May;521(1-2):77-83. doi: 10.1016/j.abb.2012.03.023., Epub 2012 Mar 27. PMID:22475449 doi:http://dx.doi.org/10.1016/j.abb.2012.03.023
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