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- PDB-9wpe: Cryo-EM structure of the insect sex pheromone receptor ApisOR22-O... -

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Basic information

Entry
Database: PDB / ID: 9wpe
TitleCryo-EM structure of the insect sex pheromone receptor ApisOR22-Orco heterocomplex bound with nepetalactone in the closed state.
Components(Odorant receptor) x 2
KeywordsMEMBRANE PROTEIN / pheromone receptor / Apo
Function / homology
Function and homology information


olfactory receptor activity / odorant binding / signal transduction / plasma membrane
Similarity search - Function
Olfactory receptor, insect / 7tm Odorant receptor
Similarity search - Domain/homology
: / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / Odorant receptor / Odorant receptor
Similarity search - Component
Biological speciesAcyrthosiphon pisum (pea aphid)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsDong, Z. / Wang, Y.D. / Guan, Z.Y. / Wang, G.R. / Yin, P.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Cell Res / Year: 2026
Title: Structural basis of sex pheromone detection in aphids.
Authors: Zhi Dong / Yidong Wang / Ying Tian / Zeyuan Guan / Minghui Bai / Bo Zhang / Zhongqiang Jia / Jinan Wu / Song Cao / Zhou Gong / Xincheng Zhao / Weihua Ma / Bing Wang / Guirong Wang / Ping Yin /
Abstract: Sex pheromones play a central role in regulating animal behavior and reproduction. In insects, these signals are perceived through specialized odorant receptors (ORs) that mediate species-specific ...Sex pheromones play a central role in regulating animal behavior and reproduction. In insects, these signals are perceived through specialized odorant receptors (ORs) that mediate species-specific communication and safeguard genetic integrity. However, the structural basis of sex pheromone detection remains largely unresolved. Here, we identified two ORs in the pea aphid Acyrthosiphon pisum, along with the conserved OR co-receptor (Orco), which together mediate recognition of the pheromone components nepetalactone and nepetalactol. Functional assays demonstrated that ApOR21-Orco and ApOR22-Orco specifically respond to nepetalactol and nepetalactone, respectively. Using cryo-electron microscopy, we resolved the structure of the ApOR22-Orco complex in three states - unbound closed, nepetalactone-bound closed, and nepetalactone-bound open - revealing a heterotetrameric ion channel formed by one ApOR22 and three ApOrco subunits. Ligand binding to ApOR22 triggers conformational rearrangements that induce asymmetric pore dilation, thereby enabling ion conduction. Together, these results provide a mechanistic framework for understanding sex pheromone perception in insects and establish a structural foundation for the rational development of environmentally sustainable pest-control strategies.
History
DepositionSep 9, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Aug 26, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 26, 2026Data content type: EM metadata / Data content type: EM metadata / 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
B: Odorant receptor
C: Odorant receptor
D: Odorant receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)214,16411
Polymers209,2574
Non-polymers4,9077
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 / OR22


Mass: 50506.777 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acyrthosiphon pisum (pea aphid) / Production host: Homo sapiens (human) / References: UniProt: A0A8R2JM50
#2: Protein Odorant receptor


Mass: 52916.766 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acyrthosiphon pisum (pea aphid) / Gene: Orco / Production host: Homo sapiens (human) / References: UniProt: A0A1S6J137
#3: Chemical ChemComp-A1EX6 / (4~{a}~{S},7~{S},7~{a}~{R})-4,7-dimethyl-5,6,7,7~{a}-tetrahydro-4~{a}~{H}-cyclopenta[c]pyran-1-one / nepetalactone cis-trans-form


Mass: 166.217 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H14O2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-PC1 / 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / 3-SN-PHOSPHATIDYLCHOLINE


Mass: 790.145 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C44H88NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
Has ligand of interestY
Has protein modificationY

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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: ApisOR22-Orco heterocomplex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Source (natural)Organism: Acyrthosiphon pisum (pea aphid)
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: 1800 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
13cryoSPARC3D reconstruction
CTF correctionType: NONE
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 209120 / Symmetry type: POINT

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