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Title | Structural basis of odor sensing by insect heteromeric odorant receptors. |
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Journal, issue, pages | Science, Vol. 384, Issue 6703, Page 1460-1467, Year 2024 |
Publish date | Jun 28, 2024 |
Authors | Jiawei Zhao / Andy Q Chen / Jaewook Ryu / Josefina Del Mármol / |
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 ...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. |
External links | Science / PubMed:38870275 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.62 - 2.95 Å |
Structure data | EMDB-42848, PDB-8v00: EMDB-42850, PDB-8v02: EMDB-42945, PDB-8v3c: EMDB-42946, PDB-8v3d: |
Chemicals | ChemComp-JZ0: PDB-1afc: |
Source |
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Keywords | MEMBRANE PROTEIN / Mosquito olfactory receptor / Mosquito olfactory receptor OR10 / Mosquitoes / Olfaction / Channel / Heterotetramer |