View source for 5zwp


==Crystal structure of the delta-class glutathione transferase from Musca domestica==
<StructureSection load='5zwp' size='340' side='right'caption='[[5zwp]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zwp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Musca_domestica Musca domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZWP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></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=5zwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zwp OCA], [https://pdbe.org/5zwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zwp RCSB], [https://www.ebi.ac.uk/pdbsum/5zwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zwp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTT1_MUSDO GSTT1_MUSDO] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Among the various glutathione transferase (GST) isozymes in insects, the delta- and epsilon-class GSTs fulfill critical functions during the detoxification of insecticides. We crystalized MdGSTD1, the major delta-class GST isozyme in the housefly (Musca domestica), in complex with glutathione (GSH) and solved its structure at a resolution of 1.4A. The overall folding of MdGSTD1 resembled other known delta-class GSTs. Its substrate binding pocket was exposed to solvent and considerably more open than in the epsilon-class GST from M. domestica (MdGSTE2). However, their C-terminal structures differed the most because of the different lengths of the C-terminal regions. Although this region does not seem to directly interact with substrates, its deletion reduced the enzymatic activity by more than 70%, indicating a function in maintaining the proper conformation of the binding pocket. Binding of GSH to the GSH-binding region of MdGSTD1 results in a rigid conformation of this region. Although MdGSTD1 has a higher affinity for GSH than the epsilon class enzymes, the thiol group of the GSH molecule was not close enough to serine residue 9 to form a hydrogen-bond with this residue, which is predicted to act as the catalytic center for thiol group deprotonation in GSH.

Crystal structure of the delta-class glutathione transferase in Musca domestica.,Sue M, Yajima S Biochem Biophys Res Commun. 2018 Jul 20;502(3):345-350. doi:, 10.1016/j.bbrc.2018.05.161. Epub 2018 May 30. PMID:29803675<ref>PMID:29803675</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zwp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Musca domestica]]
[[Category: Sue M]]
[[Category: Yajima S]]