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- EMDB-66140: Cryo-EM structure of the insect sex pheromone receptor ApisOR22-O... -

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Basic information

Entry
Database: EMDB / ID: EMD-66140
TitleCryo-EM structure of the insect sex pheromone receptor ApisOR22-Orco heterocomplex bound with nepetalactone in the closed state.
Map data
Sample
  • Complex: ApisOR22-Orco heterocomplex
    • Protein or peptide: Odorant receptor
    • Protein or peptide: Odorant receptor
  • Ligand: (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
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Keywordspheromone receptor / Apo / MEMBRANE PROTEIN
Function / homologyOlfactory receptor, insect / 7tm Odorant receptor / olfactory receptor activity / odorant binding / signal transduction / plasma membrane / Odorant receptor / Odorant receptor
Function and homology information
Biological speciesAcyrthosiphon pisum (pea aphid)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsDong Z / Wang YD / Guan ZY / Wang GR / Yin P
Funding support China, 1 items
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, 2025-
Header (metadata) releaseAug 26, 2026-
Map releaseAug 26, 2026-
UpdateAug 26, 2026-
Current statusAug 26, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_66140.png

Downloads & links

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Map

FileDownload / File: emd_66140.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 320 pix.
= 263.68 Å		0.82 Å/pix.
x 320 pix.
= 263.68 Å		0.82 Å/pix.
x 320 pix.
= 263.68 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.824 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-1.933121 - 3.4820707
Average (Standard dev.)0.0053857826 (±0.06974985)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 263.68 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_66140_half_map_1.map
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Half map: #2

Fileemd_66140_half_map_2.map
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Sample components

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Entire : ApisOR22-Orco heterocomplex

EntireName: ApisOR22-Orco heterocomplex
Components
  • Complex: ApisOR22-Orco heterocomplex
    • Protein or peptide: Odorant receptor
    • Protein or peptide: Odorant receptor
  • Ligand: (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
  • Ligand: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

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Supramolecule #1: ApisOR22-Orco heterocomplex

SupramoleculeName: ApisOR22-Orco heterocomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Acyrthosiphon pisum (pea aphid)

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Macromolecule #1: Odorant receptor

MacromoleculeName: Odorant receptor / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Acyrthosiphon pisum (pea aphid)
Molecular weightTheoretical: 50.506777 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MKDILLNSIM HRNDSWIGSK IASSAALTND GGGDEMTIHQ DNSSNERDYQ CEDGGTAMDV KLFKAIGMYQ LLHPVECGLN SDLCRKTAM MVVGLTVGLQ LMQVFRLYLA RHDIPMFANM AMLVVYGFMC LLKGYTLANH ADRICITLEV ARYAFTDCGR R DPSLMRRC ...String:
MKDILLNSIM HRNDSWIGSK IASSAALTND GGGDEMTIHQ DNSSNERDYQ CEDGGTAMDV KLFKAIGMYQ LLHPVECGLN SDLCRKTAM MVVGLTVGLQ LMQVFRLYLA RHDIPMFANM AMLVVYGFMC LLKGYTLANH ADRICITLEV ARYAFTDCGR R DPSLMRRC RARLSTILRT FVGLSFGTLV VWLVMPWFLA SEYDGKPLIW AVVYVVESII LTVNVFCWTS FDCYLVTMCF VF EAMFRTM SSGYEKVGRG QPIHPHTNQP FGDHRRSDSE VKANVTLTFP SHYDDLISHI KDNQKIVEKY KTFFEIVTPT VLL QIADGS YTIITMIFLI SIAYLNGNSI LSPMILKYVC GLVSLTIELY IFCYAFNYIE DGRSTVNFGL YSCDWTDKDL KFKK TVLLA MSMNSANKQV MKLSPNSIVN LEMFSRVMNM SYTIVSTLLS

UniProtKB: Odorant receptor

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Macromolecule #2: Odorant receptor

MacromoleculeName: Odorant receptor / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Acyrthosiphon pisum (pea aphid)
Molecular weightTheoretical: 52.916766 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGYKKDGLIK DLWPNIRLIQ LSGLFISEYY DDYSGLAVLF RKIYSWITAI IIYSQFIFIV IFMVTKSNDS DQLAAGVVTT LFFTHSMIK FVYFSTGTKS FYRTLSCWNN TSPHPLFAES HSRFHAKSLS RMRQLLIIVS IVTIFTTISW TTITFFGESV W KVPDPETF ...String:
MGYKKDGLIK DLWPNIRLIQ LSGLFISEYY DDYSGLAVLF RKIYSWITAI IIYSQFIFIV IFMVTKSNDS DQLAAGVVTT LFFTHSMIK FVYFSTGTKS FYRTLSCWNN TSPHPLFAES HSRFHAKSLS RMRQLLIIVS IVTIFTTISW TTITFFGESV W KVPDPETF NQTMYVPVPR LMLHSWYPWD SGHGLGYIVA FVLQFYWVFI TLSHSNLMEL LFSSFLVHAC EQLQHLKEIL NP LIELSAT LDSSVHNPAE IFRANSAKNQ SINGIDHDYN GSYVNEITEY GTKGENEPNR KGPNNLTSNQ EVLVRSAIKY WVE RHKHVV KYVSLITECY GSALLFHMLV STVILTILAY QATKINGVNV FAFSTIGYLM YSFAQIFMFC IHGNELIEES SSVM EAAYG CHWYDGSEEA KTFVQIVCQQ CQKPLIVSGA KFFNVSLDLF ASVLGAVVTY FMVLVQLK

UniProtKB: Odorant receptor

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Macromolecule #3: (4~{a}~{S},7~{S},7~{a}~{R})-4,7-dimethyl-5,6,7,7~{a}-tetrahydro-4...

MacromoleculeName: (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
type: ligand / ID: 3 / Number of copies: 1 / Formula: A1EX6
Molecular weightTheoretical: 166.217 Da

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Macromolecule #4: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE

MacromoleculeName: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 4 / Number of copies: 6 / Formula: PC1
Molecular weightTheoretical: 790.145 Da
Chemical component information

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 209120
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: MAXIMUM LIKELIHOOD

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