9F7K

Glutathione transferase epsilon 1 from Drosophila melanogaster in complex with glutathione

Summary for 9F7K

• Entry DOI: 10.2210/pdb9f7k/pdb
• Descriptor: GH14654p, GLYCEROL, GLUTATHIONE, ... (5 entities in total)
• Functional Keywords: glutathione, transferase, insect, epsilon
• Biological source: Drosophila melanogaster American nodavirus (ANV) SW-2009a
• Total number of polymer chains: 2
• Total formula weight: 51418.28

Authors

Didierjean, C.,Schwartz, M.,Neiers, F. (deposition date: 2024-05-03, release date: 2024-09-04)

Primary citation

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.
Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.
Biomolecules, 14:-, 2024

PubMed 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.

PubMed: 39062472
DOI: 10.3390/biom14070758

Experimental method

X-RAY DIFFRACTION (1.8 Å)