Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases

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 GS...

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Published inBiomolecules (Basel, Switzerland) Vol. 14; no. 7; p. 758
Main Authors Schwartz, Mathieu, Petiot, Nicolas, Chaloyard, Jeanne, Senty-Segault, Véronique, Lirussi, Frédéric, Senet, Patrick, Nicolai, Adrien, Heydel, Jean-Marie, Canon, Francis, Sonkaria, Sanjiv, Khare, Varsha, Didierjean, Claude, Neiers, Fabrice
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 26.06.2024
MDPI
Subjects
Amino acids
Biosynthesis
Circular dichroism
Delta GST
Dimerization
dimerization interface
Drosophila
Drosophila melanogaster
Enzymes
Glutathione
glutathione transferases
GST
Insects
Interfaces
Life Sciences
Nucleotide sequence
protein stability
Proteins
Thermal stability
Thermodynamics
Thiols
Transferases
France
United States > US
Japan
Germany
Epsilon GST
glutathione transferases
dimerization interface
GST
Delta GST
Drosophila melanogaster
protein stability
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Summary: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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ISSN:2218-273X
2218-273X
DOI:10.3390/biom14070758