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TitleCryo-EM structure of the insect olfactory receptor Orco.
Journal, issue, pagesNature, Vol. 560, Issue 7719, Page 447-452, Year 2018
Publish dateAug 15, 2018
AuthorsJoel A Butterwick / Josefina Del Mármol / Kelly H Kim / Martha A Kahlson / Jackson A Rogow / Thomas Walz / Vanessa Ruta /
PubMed AbstractThe 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 ...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.
External linksNature / PubMed:30111839 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

7352

6c70

EMDB-7352, PDB-6c70:
Cryo-EM structure of Orco
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • apocrypta bakeri (insect)
KeywordsMEMBRANE PROTEIN / Olfactory receptor / Ion channel / Insect / Fab

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