View source for 4pnf


==Glutathione S-Transferase from Drosophila melanogaster - isozyme E6==
<StructureSection load='4pnf' size='340' side='right'caption='[[4pnf]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pnf]] is a 8 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=4PNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PNF 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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pnf OCA], [https://pdbe.org/4pnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pnf RCSB], [https://www.ebi.ac.uk/pdbsum/4pnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pnf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7JZM3_DROME Q7JZM3_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytosolic glutathione transferases (GSTs) comprise a large family of enzymes with canonical structures that diverge functionally and structurally among mammals, invertebrates and plants. Whereas mammalian GSTs have been characterized extensively with regard to their structure and function, invertebrate GSTs remain relatively unstudied. The invertebrate GSTs do, however, represent potentially important drug targets for infectious diseases and agricultural applications. In addition, it is essential to fully understand the structure and function of invertebrate GSTs, which play important roles in basic biological processes. Invertebrates harbor delta- and epsilon-class GSTs, which are not found in other organisms. Drosophila melanogaster GSTs (DmGSTs) are likely to contribute to detoxication or antioxidative stress during development, but they have not been fully characterized. Here, the structures of two epsilon-class GSTs from Drosophila, DmGSTE6 and DmGSTE7, are reported at 2.1 and 1.5 A resolution, respectively, and are compared with other GSTs to identify structural features that might correlate with their biological functions. The structures of DmGSTE6 and DmGSTE7 are remarkably similar; the structures do not reveal obvious sources of the minor functional differences that have been observed. The main structural difference between the epsilon- and delta-class GSTs is the longer helix (A8) at the C-termini of the epsilon-class enzymes.

Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster.,Scian M, Le Trong I, Mazari AM, Mannervik B, Atkins WM, Stenkamp RE Acta Crystallogr D Biol Crystallogr. 2015 Oct 1;71(Pt 10):2089-98. doi:, 10.1107/S1399004715013929. Epub 2015 Sep 26. PMID:26457432<ref>PMID:26457432</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pnf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Atkins WM]]
[[Category: Le Trong I]]
[[Category: Mannervik B]]
[[Category: Scian M]]
[[Category: Stenkamp RE]]