4g0k
From Proteopedia
Revision as of 20:17, 19 October 2022
Glutathionyl-hydroquinone reductase, YqjG, of E.coli complexed with GS-menadione
Structural highlights
FunctionYQJG_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 PubMedGlutathionyl-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
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