5zwp: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 5zwp~~ is ~~ON HOLD~~

==Crystal structure of the delta-class glutathione transferase from Musca domestica==

== 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]] 1.4Å</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.

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

==See Also==

*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Musca domestica]]

[[Category: Sue M]]

[[Category: Yajima S]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5zwp is ON HOLD
+==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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]