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
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.
Mots clés
Delta GST, Drosophila melanogaster, Epsilon GST, GST, dimerization interface, glutathione transferases, protein stability
Référence
Biomolecules. 2024 06 26;14(7):