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Cryo-EM structure of the insect olfactory receptor Orco
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Cryo-EM structure of the insect olfactory receptor Orco
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Journal Article
Cryo-EM structure of the insect olfactory receptor Orco
2018
Overview
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.
A cryo-electron microscopy structure of the insect Orco subunit, which forms ion channels with diverse olfactory receptors, reveals a tetrameric cation channel and sheds light on insect olfaction.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ 82/83
/ 9/74
/ Animals
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Immunoglobulin Fab Fragments - chemistry
/ Immunoglobulin Fab Fragments - ultrastructure
/ Insects
/ Odorants
/ Protein Structure, Quaternary
/ Receptors, Odorant - chemistry
/ Receptors, Odorant - metabolism
/ Receptors, Odorant - ultrastructure
/ Science
/ Wasps
