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| | ==Glutathionyl-Hydroquinone Reductase, YqjG of Escherichia coli== | | ==Glutathionyl-Hydroquinone Reductase, YqjG of Escherichia coli== |
| - | <StructureSection load='4g0i' size='340' side='right' caption='[[4g0i]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='4g0i' size='340' side='right'caption='[[4g0i]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g0i]] 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=4G0I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G0I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g0i]] 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=4G0I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G0I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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">[[4g0k|4g0k]], [[4g0l|4g0l]]</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=4g0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g0i OCA], [https://pdbe.org/4g0i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g0i RCSB], [https://www.ebi.ac.uk/pdbsum/4g0i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g0i ProSAT]</span></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='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=4g0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g0i OCA], [http://pdbe.org/4g0i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g0i RCSB], [http://www.ebi.ac.uk/pdbsum/4g0i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g0i 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> |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Green, A R]] | + | [[Category: Large Structures]] |
| - | [[Category: Hayes, R P]] | + | [[Category: Green AR]] |
| - | [[Category: Kang, C]] | + | [[Category: Hayes RP]] |
| - | [[Category: Xun, L]] | + | [[Category: Kang C]] |
| - | [[Category: Glutathionyl-hydroquinone reductase]] | + | [[Category: Xun L]] |
| - | [[Category: Oxidoreductase]]
| + | |
| 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]
Publication Abstract from PubMed
Glutathionyl-hydroquinone reductases (GS- HQRs) are a newly identified group of glutathione transferases, and they are widely distributed in bacteria, halobacteria, fungi, and plants. GS-HQRs catalyze glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-hydroquinones) to hydroquinones. GS-hydroquinones can be spontaneously formed from benzoquinones reacting with reduced GSH via Michael addition, and GS-HQRs convert the conjugates to hydroquinones. In this report we have determined the structures of two bacterial GS-HQRs, PcpF of Sphingobium chlorophenolicum and YqjG of Escherichia coli. The two structures and the previously reported structure of a fungal GS-HQR shared many features and displayed complete conservation for all the critical residues. Furthermore, we obtained the binary complex structures with GS-menadione, which in its reduced form, GS-menadiol, is a substrate. The structure revealed a large H-site that could accommodate various substituted hydroquinones and a hydrogen network of three Tyr residues that could provide the proton for reductive deglutathionylation. Mutation of the Tyr residues and the position of two GSH molecules confirmed the proposed mechanism of GS-HQRs. The conservation of GS-HQRs across bacteria, halobacteria, fungi, and plants potentiates the physiological role of these enzymes in quinone metabolism.
Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.,Green AR, Hayes RP, Xun L, Kang C J Biol Chem. 2012 Oct 19;287(43):35838-48. doi: 10.1074/jbc.M112.395541. Epub, 2012 Sep 6. PMID:22955277[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ 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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