Structure-activity analysis suggests an olfactory function for the unique antennal delta glutathione transferase of Apis mellifera.
Apis mellifera GSTD1
antennae
glutathione transferase
odorant
stability
sulfur sandwich
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
07 Nov 2023
07 Nov 2023
Historique:
revised:
04
10
2023
received:
15
09
2023
accepted:
09
10
2023
pubmed:
7
11
2023
medline:
7
11
2023
entrez:
7
11
2023
Statut:
aheadofprint
Résumé
Glutathione transferases (GST) are detoxification enzymes that conjugate glutathione to a wide array of molecules. In the honey bee Apis mellifera, AmGSTD1 is the sole member of the delta class of GSTs, with expression in antennae. Here, we structurally and biochemically characterized AmGSTD1 to elucidate its function. We showed that AmGSTD1 can efficiently catalyse the glutathione conjugation of classical GST substrates. Additionally, AmGSTD1 exhibits binding properties with a range of odorant compounds. AmGSTD1 has a peculiar interface with a structural motif we propose to call 'sulfur sandwich'. This motif consists of a cysteine disulfide bridge sandwiched between the sulfur atoms of two methionine residues and is stabilized by CH…S hydrogen bonds and S…S sigma-hole interactions. Thermal stability studies confirmed that this motif is important for AmGSTD1 stability and, thus, could facilitate its functions in olfaction.
Identifiants
pubmed: 37933500
doi: 10.1002/1873-3468.14770
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Agence Nationale de la Recherche
ID : ANR-20-CE21-0002
Organisme : Agence Nationale de la Recherche
ID : ANR-22-CE21-0001
Informations de copyright
© 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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