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| | <StructureSection load='4wr5' size='340' side='right'caption='[[4wr5]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='4wr5' size='340' side='right'caption='[[4wr5]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wr5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WR5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wr5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WR5 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.93Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3CT:3-CHLORO-L-TYROSINE'>3CT</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3CT:3-CHLORO-L-TYROSINE'>3CT</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wr4|4wr4]]</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=4wr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wr5 OCA], [https://pdbe.org/4wr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wr5 RCSB], [https://www.ebi.ac.uk/pdbsum/4wr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wr5 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wr5 OCA], [http://pdbe.org/4wr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wr5 RCSB], [http://www.ebi.ac.uk/pdbsum/4wr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wr5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. | + | [https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Blood fluke]] | |
| - | [[Category: Glutathione transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Akasaka, R]] | + | [[Category: Schistosoma japonicum]] |
| - | [[Category: Itagaki, T]] | + | [[Category: Akasaka R]] |
| - | [[Category: Kawazoe, M]] | + | [[Category: Itagaki T]] |
| - | [[Category: Ohtake, K]] | + | [[Category: Kawazoe M]] |
| - | [[Category: Sakamoto, K]] | + | [[Category: Ohtake K]] |
| - | [[Category: Shirouzu, M]] | + | [[Category: Sakamoto K]] |
| - | [[Category: Takemoto, C]] | + | [[Category: Shirouzu M]] |
| - | [[Category: Tomabechi, Y]] | + | [[Category: Takemoto C]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Tomabechi Y]] |
| - | [[Category: Specfic site]]
| + | [[Category: Yokoyama S]] |
| - | [[Category: Alfa]]
| + | |
| - | [[Category: Alfa/beta]]
| + | |
| - | [[Category: Cytoplasmic]]
| + | |
| - | [[Category: Detoxification]]
| + | |
| - | [[Category: Gutathione]]
| + | |
| - | [[Category: Homodimeric]]
| + | |
| - | [[Category: Themostabilized structure]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Two domain]]
| + | |
| - | [[Category: Xenobiotic compound]]
| + | |
| Structural highlights
Function
GST26_SCHJA Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
Publication Abstract from PubMed
Recent advances have fundamentally changed the ways in which synthetic amino acids are incorporated into proteins, enabling their efficient and multiple-site incorporation, in addition to the 20 canonical amino acids. This development provides opportunities for fresh approaches toward addressing fundamental problems in bioengineering. In the present study, we showed that the structural stability of proteins can be enhanced by integrating bulky halogenated amino acids at multiple selected sites. Glutathione S-transferase was thus stabilized significantly (by 5.2 and 5.6 kcal/mol) with 3-chloro- and 3-bromo-l-tyrosines, respectively, incorporated at seven selected sites. X-ray crystallographic analyses revealed that the bulky halogen moieties filled internal spaces within the molecules, and formed non-canonical stabilizing interactions with the neighboring residues. This new mechanism for protein stabilization is quite simple and applicable to a wide range of proteins, as demonstrated by the rapid stabilization of the industrially relevant azoreductase.
Protein stabilization utilizing a redefined codon.,Ohtake K, Yamaguchi A, Mukai T, Kashimura H, Hirano N, Haruki M, Kohashi S, Yamagishi K, Murayama K, Tomabechi Y, Itagaki T, Akasaka R, Kawazoe M, Takemoto C, Shirouzu M, Yokoyama S, Sakamoto K Sci Rep. 2015 May 18;5:9762. doi: 10.1038/srep09762. PMID:25985257[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ohtake K, Yamaguchi A, Mukai T, Kashimura H, Hirano N, Haruki M, Kohashi S, Yamagishi K, Murayama K, Tomabechi Y, Itagaki T, Akasaka R, Kawazoe M, Takemoto C, Shirouzu M, Yokoyama S, Sakamoto K. Protein stabilization utilizing a redefined codon. Sci Rep. 2015 May 18;5:9762. doi: 10.1038/srep09762. PMID:25985257 doi:http://dx.doi.org/10.1038/srep09762
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