3mak: Difference between revisions
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==Crystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in complex with glutathione== | ==Crystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in complex with glutathione== | ||
<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 [ | <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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f6f|3f6f]], [[3gh6|3gh6]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTD1 ([ | <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'>[ | <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'>[ | <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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3mak" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3mak" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Large Structures]] | |||
[[Category: Ketterman, A J]] | [[Category: Ketterman, A J]] | ||
[[Category: Robinson, R C]] | [[Category: Robinson, R C]] | ||
Revision as of 16:45, 4 May 2022
Crystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in complex with glutathioneCrystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in complex with glutathione
Structural highlights
Function[GSTT1_DROME] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity. Publication Abstract from PubMedWe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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