8PBV
Solution NMR structure of D. melanogaster TotA
Summary for 8PBV
| Entry DOI | 10.2210/pdb8pbv/pdb |
| NMR Information | BMRB: 34825 |
| Descriptor | Protein Turandot A (1 entity in total) |
| Functional Keywords | turandot, antimicrobial peptide, tota, stress, unknown function |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 12989.51 |
| Authors | |
| Primary citation | Rommelaere, S.,Carboni, A.,Bada Juarez, J.F.,Boquete, J.P.,Abriata, L.A.,Teixeira Pinto Meireles, F.,Rukes, V.,Vincent, C.,Kondo, S.,Dionne, M.S.,Dal Peraro, M.,Cao, C.,Lemaitre, B. A humoral stress response protects Drosophila tissues from antimicrobial peptides. Curr.Biol., 34:1426-1437.e6, 2024 Cited by PubMed Abstract: 7An efficient immune system must provide protection against a broad range of pathogens without causing excessive collateral tissue damage. While immune effectors have been well characterized, we know less about the resilience mechanisms protecting the host from its own immune response. Antimicrobial peptides (AMPs) are small, cationic peptides that contribute to innate defenses by targeting negatively charged membranes of microbes. While protective against pathogens, AMPs can be cytotoxic to host cells. Here, we reveal that a family of stress-induced proteins, the Turandots, protect the Drosophila respiratory system from AMPs, increasing resilience to stress. Flies lacking Turandot genes are susceptible to environmental stresses due to AMP-induced tracheal apoptosis. Turandot proteins bind to host cell membranes and mask negatively charged phospholipids, protecting them from cationic pore-forming AMPs. Collectively, these data demonstrate that Turandot stress proteins mitigate AMP cytotoxicity to host tissues and therefore improve their efficacy. PubMed: 38484734DOI: 10.1016/j.cub.2024.02.049 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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