10HA
Crystal Structure of Honeybee (Apis mellifera) omega class glutathione S-transferase AmGST-O1
Summary for 10HA
| Entry DOI | 10.2210/pdb10ha/pdb |
| Related PRD ID | PRD_002593 |
| Descriptor | Pyrimidodiazepine synthase, Glutathione (3 entities in total) |
| Functional Keywords | glutathione, complex, honey bee, omega, gst, glutathione s-transferase, transferase |
| Biological source | Apis mellifera (honey bee) |
| Total number of polymer chains | 4 |
| Total formula weight | 120722.14 |
| Authors | |
| Primary citation | Koirala, S.,Moural, T.W.,Bhattarai, G.,Phan, N.T.,Rajotte, E.G.,Biddinger, D.J.,Zhu, F. Structural and Functional Insights into a Honey Bee Omega-Class Glutathione S-Transferase Mediating Chemical Sequestration and Antioxidative Stress. J.Agric.Food Chem., 2026 Cited by PubMed Abstract: The European honey bee ( L.) is an essential crop pollinator and is frequently exposed to pesticide residues that may compromise bee health. Mechanisms underlying chemical adaptation and detoxification in honey bees remain incompletely understood, particularly those involving glutathione S-transferases (GSTs). Here, we structurally and functionally characterized omega-class GST AmGSTO1. was highly expressed in the fat bodies of nurse and forager bees. X-ray crystallography resolved the glutathione (GSH)-bound AmGSTO1 structure, revealing an active-site cysteine characteristic of omega GSTs. Enzyme assays showed greater catalytic efficiency toward the thioltransferase substrate HED than toward CDNB or PNA. Disc diffusion and bacterial survival assays demonstrated antioxidant activity against cumene hydroperoxide, hydrogen peroxide, and paraquat. Fluorescence binding assays indicated agrochemical binding, while HPLC detected no significant substrate depletion, suggesting a sequestration rather than catalytic role. Overall, AmGSTO1 may contribute to the protection against agrochemical toxicity and oxidative stress in honey bees. PubMed: 42205059DOI: 10.1021/acs.jafc.6c03265 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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