|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6riv' size='340' side='right'caption='[[6riv]], [[Resolution|resolution]] 1.33Å' scene=''> | | <StructureSection load='6riv' size='340' side='right'caption='[[6riv]], [[Resolution|resolution]] 1.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6riv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RIV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6riv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alopecurus_myosuroides Alopecurus myosuroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RIV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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]] 1.33Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GS8:S-HYDROXY-GLUTATHIONE'>GS8</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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=6riv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6riv OCA], [https://pdbe.org/6riv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6riv RCSB], [https://www.ebi.ac.uk/pdbsum/6riv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6riv 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=6riv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6riv OCA], [http://pdbe.org/6riv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6riv RCSB], [http://www.ebi.ac.uk/pdbsum/6riv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6riv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9ZS17_ALOMY Q9ZS17_ALOMY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6riv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6riv" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutathione transferase]] | + | [[Category: Alopecurus myosuroides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Papageorgiou, A C]] | + | [[Category: Papageorgiou AC]] |
| - | [[Category: Poudel, N]] | + | [[Category: Poudel N]] |
| - | [[Category: Detoxification]]
| + | |
| - | [[Category: Glutathione]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xenobiotic]]
| + | |
| Structural highlights
6riv is a 2 chain structure with sequence from Alopecurus myosuroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.33Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q9ZS17_ALOMY
Publication Abstract from PubMed
Multiple-herbicide resistant (MHR) weeds are a global problem and a looming threat to weed control in crops. MHR weeds express a specific phi class glutathione transferase (MHR-GSTF) which seems to contribute to herbicide resistance. The present work aims to investigate the structure and catalytic properties of the MHR-GSTFs from different grass weeds and crops (Alopecurus myosuroides, Lolium rigidum, Hordeum vulgare, Triticum aestivum). Recombinant MHR-GSTFs were expressed in E. coli and purified by affinity chromatography. Kinetic analysis of substrate specificity using a range of thiol substrates and xenobiotic compounds suggested that all enzymes display a broad range of specificity and are capable of detoxifying major stress-induced toxic products. Notably, all tested enzymes exhibited high activity towards organic hydroperoxides. The crystal structure of MHR-GSTF from Alopecurus myosuroides (AmGSTF) was determined by molecular replacement at 1.33 A resolution. The enzyme was resolved with bound glutathione sulfenic acid (GSOH) at the G-site and succinic acid at the H-site. The enzyme shows conserved structural features compared to other Phi class GSTs. However, some differences were observed at the C-terminal helix H9 that may affect substrate specificity. The structural and functional features of AmGSTF were compared with those of the homologue crop enzymes (HvGSTF and TaGSTF) and discussed in light of their contribution to the MHR mechanism.
Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops.,Georgakis N, Poudel N, Papageorgiou AC, Labrou NE Plant Physiol Biochem. 2020 Feb 20;149:266-276. doi:, 10.1016/j.plaphy.2020.02.012. PMID:32088578[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Georgakis N, Poudel N, Papageorgiou AC, Labrou NE. Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops. Plant Physiol Biochem. 2020 Feb 20;149:266-276. doi:, 10.1016/j.plaphy.2020.02.012. PMID:32088578 doi:http://dx.doi.org/10.1016/j.plaphy.2020.02.012
|
