8V3C
AgamOR28 structure without ligand
Summary for 8V3C
| Entry DOI | 10.2210/pdb8v3c/pdb |
| EMDB information | 42945 |
| Descriptor | OR28, Odorant receptor Orco (2 entities in total) |
| Functional Keywords | mosquitoes, olfaction, channel, heterotetramer, membrane protein |
| Biological source | Anopheles gambiae (African malaria mosquito) More |
| Total number of polymer chains | 4 |
| Total formula weight | 205441.76 |
| Authors | Zhao, J.,del Marmol, J. (deposition date: 2023-11-27, release date: 2024-06-19, Last modification date: 2024-07-10) |
| Primary citation | Zhao, J.,Chen, A.Q.,Ryu, J.,Del Marmol, J. Structural basis of odor sensing by insect heteromeric odorant receptors. Science, 384:1460-1467, 2024 Cited by PubMed Abstract: Most insects, including human-targeting mosquitoes, detect odors through odorant-activated ion channel complexes consisting of a divergent odorant-binding subunit (OR) and a conserved co-receptor subunit (Orco). As a basis for understanding how odorants activate these heteromeric receptors, we report here cryo-electron microscopy structures of two different heteromeric odorant receptor complexes containing ORs from disease-vector mosquitos or . These structures reveal an unexpected stoichiometry of one OR to three Orco subunits. Comparison of structures in odorant-bound and unbound states indicates that odorant binding to the sole OR subunit is sufficient to open the channel pore, suggesting a mechanism of OR activation and a conceptual framework for understanding evolution of insect odorant receptor sensitivity. PubMed: 38870275DOI: 10.1126/science.adn6384 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.62 Å) |
Structure validation
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