Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.

Fiche publication

Date publication

juin 2024

Journal

Biomolecules

Auteurs

Membres identifiés du Cancéropôle Est :
Pr LIRUSSI Frédéric

Tous les auteurs :
Schwartz M, Petiot N, Chaloyard J, Senty-Segault V, Lirussi F, Senet P, Nicolai A, Heydel JM, Canon F, Sonkaria S, Khare V, Didierjean C, Neiers F

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/39062472

Résumé

This study presents a comprehensive analysis of the dimerization interfaces of fly GSTs through sequence alignment. Our investigation revealed GSTE1 as a particularly intriguing target, providing valuable insights into the variations within Delta and Epsilon GST interfaces. The X-ray structure of GSTE1 was determined, unveiling remarkable thermal stability and a distinctive dimerization interface. Utilizing circular dichroism, we assessed the thermal stability of GSTE1 and other Drosophila GSTs with resolved X-ray structures. The subsequent examination of GST dimer stability correlated with the dimerization interface supported by findings from X-ray structural analysis and thermal stability measurements. Our discussion extends to the broader context of GST dimer interfaces, offering a generalized perspective on their stability. This research enhances our understanding of the structural and thermodynamic aspects of GST dimerization, contributing valuable insights to the field.