Schwartz, M., Petiot, N., Chaloyard, J., Senty-Segault, V., Lirussi, F., Senet, P., Nicolai, A., Heydel, J.M., Canon, F., Sonkaria, S., Khare, V., Didierjean, C., Neiers, F. (2024). Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.  Biomolecules 14(7): 758.

FBrf0260021

Research paper

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.

PMC11274453 (PMC) (EuropePMC)