8Q8A

Crystal structure of Apis mellifera glutathione transferase delta 1, mutant M126L

Summary for 8Q8A

• Entry DOI: 10.2210/pdb8q8a/pdb
• Descriptor: Glutathione S-transferase D1 isoform X1, SULFATE ION (3 entities in total)
• Functional Keywords: glutathione transferase, detoxification, transferase
• Biological source: Apis mellifera (honey bee)
• Total number of polymer chains: 1
• Total formula weight: 25163.96

Authors

Schwartz, M.,Neiers, F. (deposition date: 2023-08-18, release date: 2023-10-18, Last modification date: 2024-01-10)

Primary citation

Schwartz, M.,Boichot, V.,Muradova, M.,Fournier, P.,Senet, P.,Nicolai, A.,Canon, F.,Lirussi, F.,Ladeira, R.,Maibeche, M.,Chertemps, T.,Aubert, E.,Didierjean, C.,Neiers, F.
Structure-activity analysis suggests an olfactory function for the unique antennal delta glutathione transferase of Apis mellifera.
Febs Lett., 597:3038-3048, 2023

PubMed Abstract: 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.

PubMed: 37933500
DOI: 10.1002/1873-3468.14770

Experimental method

X-RAY DIFFRACTION (1.75 Å)