9s3a

From Proteopedia

TaGST-10 in complex with deoxynivalenol-13-glutathione

Structural highlights

9s3a is a 2 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A3B5XZG4_WHEAT Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.[RuleBase:RU369102]

Publication Abstract from PubMed

Deoxynivalenol (DON) is a toxicologically relevant trichothecene mycotoxin frequently found in cereal products. It is a virulence factor produced by the plant pathogen Fusarium graminearum during cereal crop infections. Investigating plant defense mechanisms is crucial for understanding plant resistance to F. graminearum and identifying new biocatalysts for DON detoxification. Previous studies identified DON-thiol adducts in cereal samples, indicating partial DON detoxification by glutathione transferases (GSTs). DON possesses two electrophilic centers for thiol conjugation, resulting in either epoxide opening at C13 or Michael addition at C10. At present, information on plant GSTs that catalyze these reactions is limited. In this study, Fusarium-inducible wheat GSTs were identified by analyzing the transcriptome of Fusarium-infected wheat heads. Twelve highly induced genes of the tau and phi GST classes were heterologously expressed and purified, biochemically characterized with model substrates, and assayed for activity with DON. Use of liquid chromatography coupled to mass spectrometry showed that four of the selected tau class GSTs conjugated DON to glutathione (GSH) by epoxide opening (DON-13-GSH) and/or the reversible Michael addition reaction (DON-10-GSH). The crystal structure of a wheat GST (herein designated "TaGST-10") in complex with DON-13-GSH was solved at a resolution of 2.3 A and provided insights into the binding of DON at the active site of tau class GSTs. Our results corroborate the hypothesis that enzyme-catalyzed, glutathione-mediated DON detoxification may be involved in plant response to Fusarium infection.

Detoxification of deoxynivalenol by pathogen-inducible tau-class glutathione transferases from wheat.,Michlmayr H, Siller M, Kenjeric L, Doppler M, Malachova A, Hofer M, Hametner C, Schweiger W, Steiner B, Kugler KG, Mayer KFX, Buerstmayr H, Schuhmacher R, Krska R, Labrou NE, Papageorgiou AC, Adam G J Biol Chem. 2025 Aug 14:110600. doi: 10.1016/j.jbc.2025.110600. PMID:40818610^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Michlmayr H, Siller M, Kenjeric L, Doppler M, Malachova A, Hofer M, Hametner C, Schweiger W, Steiner B, Kugler KG, Mayer KFX, Buerstmayr H, Schuhmacher R, Krska R, Labrou NE, Papageorgiou AC, Adam G. Detoxification of deoxynivalenol by pathogen-inducible tau-class glutathione transferases from wheat. J Biol Chem. 2025 Aug 14:110600. PMID:40818610 doi:10.1016/j.jbc.2025.110600