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| | ==The glutathione bound structure of YqjG, a glutathione transferase homolog from Escherichia coli K-12== | | ==The glutathione bound structure of YqjG, a glutathione transferase homolog from Escherichia coli K-12== |
| - | <StructureSection load='3r3e' size='340' side='right' caption='[[3r3e]], [[Resolution|resolution]] 2.21Å' scene=''> | + | <StructureSection load='3r3e' size='340' side='right'caption='[[3r3e]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3r3e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R3E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3r3e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R3E 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]] 2.205Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3102, JW3073, yqjG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3r3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r3e OCA], [https://pdbe.org/3r3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r3e RCSB], [https://www.ebi.ac.uk/pdbsum/3r3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r3e 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=3r3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r3e OCA], [http://pdbe.org/3r3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r3e RCSB], [http://www.ebi.ac.uk/pdbsum/3r3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r3e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YQJG_ECOLI YQJG_ECOLI]] Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2-hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4-dinitrobenzene (CDNB).<ref>PMID:20388120</ref> <ref>PMID:22686328</ref> <ref>PMID:22955277</ref> | + | [https://www.uniprot.org/uniprot/YQJG_ECOLI YQJG_ECOLI] Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2-hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4-dinitrobenzene (CDNB).<ref>PMID:20388120</ref> <ref>PMID:22686328</ref> <ref>PMID:22955277</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Glutathione transferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Armstrong, R N]] | + | [[Category: Armstrong RN]] |
| - | [[Category: Branch, M C]] | + | [[Category: Branch MC]] |
| - | [[Category: Cook, P D]] | + | [[Category: Cook PD]] |
| - | [[Category: Harp, J M]] | + | [[Category: Harp JM]] |
| - | [[Category: Disulfide bond reductase]]
| + | |
| - | [[Category: Glutathione]]
| + | |
| - | [[Category: Gst]]
| + | |
| - | [[Category: Thioredoxin domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
YQJG_ECOLI Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2-hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4-dinitrobenzene (CDNB).[1] [2] [3]
References
- ↑ Xun L, Belchik SM, Xun R, Huang Y, Zhou H, Sanchez E, Kang C, Board PG. S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases. Biochem J. 2010 May 27;428(3):419-27. doi: 10.1042/BJ20091863. PMID:20388120 doi:http://dx.doi.org/10.1042/BJ20091863
- ↑ Lam LK, Zhang Z, Board PG, Xun L. Reduction of benzoquinones to hydroquinones via spontaneous reaction with glutathione and enzymatic reaction by S-glutathionyl-hydroquinone reductases. Biochemistry. 2012 Jun 26;51(25):5014-21. doi: 10.1021/bi300477z. Epub 2012 Jun, 13. PMID:22686328 doi:http://dx.doi.org/10.1021/bi300477z
- ↑ Green AR, Hayes RP, Xun L, Kang C. Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases. J Biol Chem. 2012 Oct 19;287(43):35838-48. doi: 10.1074/jbc.M112.395541. Epub, 2012 Sep 6. PMID:22955277 doi:http://dx.doi.org/10.1074/jbc.M112.395541
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