4fqu
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fqu]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_chlorophenolicum Sphingobium chlorophenolicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQU FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fqu]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_chlorophenolicum Sphingobium chlorophenolicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQU FirstGlance]. <br> | ||
| - | </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=4fqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqu OCA], [https://pdbe.org/4fqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fqu RCSB], [https://www.ebi.ac.uk/pdbsum/4fqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqu ProSAT]</span></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]] 3Å</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=4fqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqu OCA], [https://pdbe.org/4fqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fqu RCSB], [https://www.ebi.ac.uk/pdbsum/4fqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PCPF_SPHCR PCPF_SPHCR] Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can act on halogenated substrates such as GS-2,6-dichloro-p-hydroquinone (GS-DiCH) and GS-trichloro-p-hydroquinone (GS-TriCH). Involved in the degradation of pentachlorophenol (PCP), a toxic pollutant.<ref>PMID:18820023</ref> | [https://www.uniprot.org/uniprot/PCPF_SPHCR PCPF_SPHCR] Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can act on halogenated substrates such as GS-2,6-dichloro-p-hydroquinone (GS-DiCH) and GS-trichloro-p-hydroquinone (GS-TriCH). Involved in the degradation of pentachlorophenol (PCP), a toxic pollutant.<ref>PMID:18820023</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:22955277</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4fqu" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Glutathionyl-Hydroquinone Reductase PcpF of Sphingobium chlorophenolicum
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