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| | <StructureSection load='1v2a' size='340' side='right'caption='[[1v2a]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1v2a' size='340' side='right'caption='[[1v2a]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v2a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_(cellia)_dirus Anopheles (cellia) dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1V2A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V2A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jlv|1jlv]], [[1jlw|1jlw]], [[1r5a|1r5a]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AdGST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7168 Anopheles (Cellia) dirus])</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=1v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v2a OCA], [https://pdbe.org/1v2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v2a RCSB], [https://www.ebi.ac.uk/pdbsum/1v2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v2a 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://proteopedia.org/fgij/fg.htm?mol=1v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v2a OCA], [http://pdbe.org/1v2a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v2a RCSB], [http://www.ebi.ac.uk/pdbsum/1v2a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v2a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9BHB0_9DIPT Q9BHB0_9DIPT] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutathione transferase]] | + | [[Category: Anopheles dirus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oakley, A J]] | + | [[Category: Oakley AJ]] |
| - | [[Category: Detoxification]]
| + | |
| - | [[Category: Glutathione]]
| + | |
| - | [[Category: Glutathione s-transferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xenobiotic]]
| + | |
| Structural highlights
Function
Q9BHB0_9DIPT
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.
Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme.,Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:15717864[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ. Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme. Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:15717864 doi:10.1042/BJ20042015
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