6C70

Cryo-EM structure of Orco

6C70 の概要

• エントリーDOI: 10.2210/pdb6c70/pdb
• EMDBエントリー: 7352
• 分子名称: Odorant receptor (1 entity in total)
• 機能のキーワード: olfactory receptor, ion channel, insect, fab, membrane protein
• 由来する生物種: Apocrypta bakeri
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 214052.95

構造登録者

Butterwick, J.A.,Kim, K.H.,Walz, T.,Ruta, V. (登録日: 2018-01-19, 公開日: 2018-08-22, 最終更新日: 2025-06-04)

主引用文献

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

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: 30111839
DOI: 10.1038/s41586-018-0420-8

実験手法

ELECTRON MICROSCOPY (3.5 Å)