6C70
Cryo-EM structure of Orco
Summary for 6C70
| Entry DOI | 10.2210/pdb6c70/pdb |
| EMDB information | 7352 |
| Descriptor | Odorant receptor (1 entity in total) |
| Functional Keywords | olfactory receptor, ion channel, insect, fab, membrane protein |
| Biological source | Apocrypta bakeri |
| Total number of polymer chains | 4 |
| Total formula weight | 214052.95 |
| Authors | Butterwick, J.A.,Kim, K.H.,Walz, T.,Ruta, V. (deposition date: 2018-01-19, release date: 2018-08-22, Last modification date: 2025-06-04) |
| Primary citation | Butterwick, J.A.,Del Marmol, J.,Kim, K.H.,Kahlson, M.A.,Rogow, J.A.,Walz, T.,Ruta, V. Cryo-EM structure of the insect olfactory receptor Orco. Nature, 560:447-452, 2018 Cited by PubMed Abstract: The olfactory system must recognize and discriminate amongst an enormous variety of chemicals in the environment. To contend with such diversity, insects have evolved a family of odorant-gated ion channels comprised of a highly conserved co-receptor (Orco) and a divergent odorant receptor (OR) that confers chemical specificity. Here, we present the single-particle cryo-electron microscopy structure of an Orco homomer from the parasitic fig wasp Apocrypta bakeri at 3.5 Å resolution, providing structural insight into this receptor family. Orco possesses a novel channel architecture, with four subunits symmetrically arranged around a central pore that diverges into four lateral conduits that open to the cytosol. The Orco tetramer has few inter-subunit interactions within the membrane and is bound together by a small cytoplasmic anchor domain. The minimal sequence conservation among ORs maps largely to the pore and anchor domain, shedding light on how the architecture of this receptor family accommodates its remarkable sequence diversity and facilitates the evolution of odour tuning. PubMed: 30111839DOI: 10.1038/s41586-018-0420-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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