Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases

Overview

Journal Biomolecules

Publisher MDPI

Specialties Biochemistry
Molecular Biology

Date 2024 Jul 27

PMID 39062472

Authors

Mathieu Schwartz

Nicolas Petiot

Jeanne Chaloyard

Veronique Senty-Segault

Frederic Lirussi

Patrick Senet

Adrien Nicolai

Jean-Marie Heydel

Francis Canon

Sanjiv Sonkaria

Varsha Khare

Claude Didierjean

Fabrice Neiers

Affiliations

Soon will be listed here.

Abstract

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.

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