|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='3qaw' size='340' side='right'caption='[[3qaw]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3qaw' size='340' side='right'caption='[[3qaw]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qaw]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QAW FirstGlance]. <br> | + | <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='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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qav|3qav]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://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'>[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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qaw OCA], [http://pdbe.org/3qaw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qaw RCSB], [http://www.ebi.ac.uk/pdbsum/3qaw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qaw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B9VX79_LATEL B9VX79_LATEL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutathione transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Laternula elliptica]] | | [[Category: Laternula elliptica]] |
| - | [[Category: Chi, Y M]] | + | [[Category: Chi YM]] |
| - | [[Category: Moon, J H]] | + | [[Category: Moon JH]] |
| - | [[Category: Park, A K]] | + | [[Category: Park AK]] |
| - | [[Category: Cytosol]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
B9VX79_LATEL
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Park AK, Moon JH, Jang EH, Park H, Ahn IY, Lee KS, Chi YM. The structure of a shellfish specific GST class glutathione S-transferase from antarctic bivalve Laternula elliptica reveals novel active site architecture. Proteins. 2013 Mar;81(3):531-7. doi: 10.1002/prot.24208. Epub 2012 Dec 24. PMID:23152139 doi:http://dx.doi.org/10.1002/prot.24208
|
