8q89

Crystal structure of Apis mellifera glutathione transferase delta 1 in a covalent dimeric state

spinqualitylabelsall models 8q89, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8q89 is a 1 chain structure with sequence from Apis mellifera. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A7M7GUY7_APIME Publication Abstract from PubMed 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. Structure-activity analysis suggests an olfactory function for the unique antennal delta glutathione transferase of Apis mellifera.,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 FEBS Lett. 2023 Dec;597(24):3038-3048. doi: 10.1002/1873-3468.14770. Epub 2023 , Nov 7. PMID:37933500 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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