9VQS

The structure of DbOR67d-DbOrco in the apo-like state

Summary for 9VQS

• Entry DOI: 10.2210/pdb9vqs/pdb
• EMDB information: 65275
• Descriptor: odorant receptor 67d-like in Drosophila bipectinata, odorant receptor coreceptor in Drosophila bipectinata (2 entities in total)
• Functional Keywords: odorant receptor; complex;channel, membrane protein
• Biological source: Drosophila bipectinata; More
• Total number of polymer chains: 4
• Total formula weight: 207240.76

Authors

Wang, J.,Guo, J. (deposition date: 2025-07-05, release date: 2026-07-01)

Primary citation

Wang, J.,Yang, C.,Chang, S.,Jiao, D.,Lin, J.,Yang, X.,Cai, W.,Ma, D.,Ding, Z.J.,Huang, J.,Huang, J.,Fan, M.,Hu, M.,Wang, Y.,Xu, H.,Su, N.,Guo, J.
Cryo-EM structures of Drosophila OR67d-Orco complexes reveal insect pheromone sensing mechanism.
Cell Res., 2026

PubMed Abstract: Pheromones mediate intraspecific communication to regulate the physiology and behavior of animals, particularly insects. The detection of pheromones is initiated by the binding of pheromone molecules, e.g., 11-cis-vaccenyl acetate (cVA) in Drosophila, to specific receptor proteins in chemosensory neurons, but the underlying molecular mechanisms remain unclear. Here, we report structures of Drosophila pheromone receptor OR67d-Orco complexes in apo closed, pheromone-bound open, and synthetic agonist VUAA1-bound open conformations. OR67d and Orco assemble into a hetero-tetrameric channel with a 1:3 stoichiometry. In OR67d, the inverted L-shaped cVA or its analog binds into a deep and bent hydrophobic pocket, inducing both local and global conformational changes that lead to an asymmetrical opening of the channel gate. By comparison, VUAA1 binds to Orco instead of OR67d to cause a similar asymmetrical opening. Together, our studies reveal the structural basis for pheromone activation of hetero-tetrameric pheromone receptors.

PubMed: 42270979
DOI: 10.1038/s41422-026-01264-2

Experimental method

ELECTRON MICROSCOPY (2.8 Å)