8ax2 | pdb_00008ax2

Crystal structure of Trametes versicolor glutathione transferase Omega 3S in complex with glutathione and pentachloro-nitrosyl-osmate

spinqualitylabelsall models 8ax2, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ax2 is a 2 chain structure with sequence from Trametes versicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL, GSH, OS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A384E145_TRAVE Publication Abstract from PubMed Glutathione transferases are detoxification enzymes with multifaceted roles, including a role in the metabolism and scavenging of nitric oxide (NO) compounds in cells. Here, we explored the ability of Trametes versicolor glutathione transferases (GSTs) from the Omega class (TvGSTOs) to bind metal-nitrosyl compounds. TvGSTOs have been studied previously for their ligandin role and are interesting models to study protein‒ligand interactions. First, we determined the X-ray structure of the TvGSTO3S isoform bound to the dinitrosyl glutathionyl iron complex (DNGIC), a physiological compound involved in the storage of nitric oxide. Our results suggested a different binding mode compared to the one previously described in human GST Pi 1 (GSTP1). Then, we investigated the manner in which TvGSTO3S binds three nonphysiological metal-nitrosyl compounds with different metal cores (iron, ruthenium and osmium). We assayed sodium nitroprusside, a well-studied vasodilator used in cases of hypertensive crises or heart failure. Our results showed that the tested GST can bind metal-nitrosyls at two distinct binding sites. Thermal shift analysis with six isoforms of TvGSTOs identified TvGSTO6S as the best interactant. Using the Griess method, TvGSTO6S was found to improve the release of nitric oxide from sodium nitroprusside in vitro, whereas the effects of human GST alpha 1 (GSTA1) and GSTP1 were moderate. Our results open new structural perspectives for understanding the interactions of glutathione transferases with metal-nitrosyl compounds associated with the biochemical mechanisms of NO uptake/release in biological systems. Structural insights into the interactions of glutathione transferases with a nitric oxide carrier and sodium nitroprusside.,Schwartz M, Perrot T, Beurton J, Zannini F, Morel-Rouhier M, Gelhaye E, Neiers F, Schaniel D, Favier F, Jacquot JP, Leroy P, Clarot I, Boudier A, Didierjean C Biochem Biophys Res Commun. 2023 Mar 15;649:79-86. doi: , 10.1016/j.bbrc.2023.01.099. Epub 2023 Feb 1. PMID:36758482 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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