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- PDB-9vqp: The structure of DmOR67d-DmOrco in the cVA-bound state -

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Basic information

Entry
Database: PDB / ID: 9vqp
TitleThe structure of DmOR67d-DmOrco in the cVA-bound state
Components
  • Odorant receptor 67d
  • Odorant receptor coreceptor
KeywordsMEMBRANE PROTEIN / Odorant Receptor / Complex / channel
Function / homology
Function and homology information


detection of pheromone / ionotropic olfactory receptor activity / sensory dendrite / olfactory receptor activity / response to pheromone / courtship behavior / detection of chemical stimulus involved in sensory perception of smell / olfactory behavior / odorant binding / cation channel complex ...detection of pheromone / ionotropic olfactory receptor activity / sensory dendrite / olfactory receptor activity / response to pheromone / courtship behavior / detection of chemical stimulus involved in sensory perception of smell / olfactory behavior / odorant binding / cation channel complex / behavioral response to ethanol / intracellularly gated calcium channel activity / coreceptor activity / dendrite membrane / sensory perception of smell / regulation of protein localization / calmodulin binding / cilium / dendrite / signal transduction / protein homodimerization activity / plasma membrane
Similarity search - Function
Olfactory receptor, insect / 7tm Odorant receptor
Similarity search - Domain/homology
(Z)-OCTADEC-11-ENYL ACETATE / Odorant receptor coreceptor / Odorant receptor 67d
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsWang, J. / Guo, J.
Funding support China, 1items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2020YFA0908501 China
CitationJournal: Cell Res / Year: 2026
Title: Cryo-EM structures of Drosophila OR67d-Orco complexes reveal insect pheromone sensing mechanism.
Authors: Jiangqin Wang / Chuanyan Yang / Shenghai Chang / Dian Jiao / Jiahao Lin / Xiaotong Yang / Weijie Cai / Demin Ma / Zhong Jie Ding / Jia Huang / Jianhua Huang / Minrui Fan / Meiqin Hu / Yong ...Authors: Jiangqin Wang / Chuanyan Yang / Shenghai Chang / Dian Jiao / Jiahao Lin / Xiaotong Yang / Weijie Cai / Demin Ma / Zhong Jie Ding / Jia Huang / Jianhua Huang / Minrui Fan / Meiqin Hu / Yong Wang / Haoxing Xu / Nannan Su / Jiangtao Guo /
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 ...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.
History
DepositionJul 5, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jul 8, 2026Provider: repository / Type: Initial release
Revision 1.0Jul 8, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 8, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 8, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jul 8, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 8, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Odorant receptor 67d
B: Odorant receptor coreceptor
C: Odorant receptor coreceptor
D: Odorant receptor coreceptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)213,0165
Polymers212,7054
Non-polymers3111
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Odorant receptor 67d


Mass: 45925.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: Or67d, CG14157 / Production host: Homo sapiens (human) / References: UniProt: Q9VT92
#2: Protein Odorant receptor coreceptor / Odorant receptor 83b


Mass: 55593.195 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: Orco, A45, Or83b, CG10609 / Production host: Homo sapiens (human) / References: UniProt: Q9VNB5
#3: Chemical ChemComp-VA / (Z)-OCTADEC-11-ENYL ACETATE


Mass: 310.515 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C20H38O2 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: The structure of DmOR67d-DmOrco in the cVA-bound state
Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Source (natural)Organism: Drosophila melanogaster (fruit fly)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k)

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Processing

EM software
IDNameVersionCategory
1RELION3.1particle selection
13RELION3.13D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 196898 / Symmetry type: POINT

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