View source for 3qaw


==Crystal structure of a glutathione-S-transferase from Antarctic clam Laternula elliptica in a complex with glutathione==
<StructureSection load='3qaw' size='340' side='right'caption='[[3qaw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qaw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Laternula_elliptica Laternula elliptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QAW 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]] 2.2&#8491;</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=3qaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qaw OCA], [https://pdbe.org/3qaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qaw RCSB], [https://www.ebi.ac.uk/pdbsum/3qaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qaw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B9VX79_LATEL B9VX79_LATEL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutathione-S-transferases have been identified in all the living species examined so far, yet little is known about their function in marine organisms. In a previous report, the recently identified GST from Antarctic bivalve Laternula elliptica (LeGST) was classified into the rho class GST, but there are several unique features of LeGST that may justify reclassification, which could represent specific shellfish GSTs. Here, we determined the crystal structure of LeGST, which is a shellfish specific class of GST. The structural analysis showed that the relatively open and wide hydrophobic H-site of the LeGST allows this GST to accommodate various substrates. These results suggest that the H-site of LeGST may be the result of adaptation to their environments as sedentary organisms. Proteins 2013. (c) 2012 Wiley Periodicals, Inc.

The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture.,Park AK, Moon JH, Jang EH, Park H, Ahn IY, Lee KS, Chi YM Proteins. 2013 Mar;81(3):531-7. doi: 10.1002/prot.24208. Epub 2012 Dec 24. PMID:23152139<ref>PMID:23152139</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qaw" 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: Laternula elliptica]]
[[Category: Chi YM]]
[[Category: Moon JH]]
[[Category: Park AK]]