9JJD
Structural analysis of autophagy-related protein 8a in Drosophila melanogaster
Summary for 9JJD
| Entry DOI | 10.2210/pdb9jjd/pdb |
| Descriptor | Autophagy-related 8a, isoform A (2 entities in total) |
| Functional Keywords | lipid tramsport, lipid binding protein, lipid transport |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 14416.56 |
| Authors | Zhang, S.Q.,Luo, X.,Wu, D.X.,Liu, J.,Li, X.Y. (deposition date: 2024-09-13, release date: 2025-03-26, Last modification date: 2025-04-09) |
| Primary citation | Zhang, S.,Luo, X.,Yuan, X.,Wu, D.,Liu, J.,Zhao, K.,Xu, Y.,Zhou, J.,Li, X.,Li, Q.X. Crystal Structure of Autophagy-Associated Protein 8 at 1.36 angstrom Resolution and Its Inhibitory Interactions with Indole Analogs. J.Agric.Food Chem., 73:7111-7120, 2025 Cited by PubMed Abstract: Autophagy-associated protein 8 (ATG8) is essential for autophagy and organismal growth and development. In this study, we successfully resolved the crystal structure of () ATG8a (ATG8a) at 1.36 Å resolution. Being distinct from previously characterized ATG8 homologues, ATG8a (121 residues) adopts a unique fold comprising five α-helices and four β-folding strands, in contrast to the canonical four α-helices and four β-folding strands observed in other ATG8 proteins. ATG8a features two active cavities: hydrophobic pocket 1 (HP1) and hydrophobic pocket 2 (HP2), which are essential for the normal physiological function of ATG8. Indole and its analogs can bind specifically with HP1. Microscale thermophoresis results demonstrated a strong affinity of 6-fluoroindole with ATG8a (3.54 μmol/L), but no affinity with the ATG8a mutant, suggesting that Lys48 is critical in binding 6-fluoroindole probably via a hydrogen bond interaction. The half-maximum lethal concentration (LC) of 6-fluoroindole against adult flies was 169 μg/mL. Our findings establish ATG8a as a promising target for developing indole-based insecticides. PubMed: 40066832DOI: 10.1021/acs.jafc.4c11205 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.36 Å) |
Structure validation
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