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- PDB-8z9a: Cryo-EM structure of the insect olfactory receptor OR5-Orco heter... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8z9a | ||||||
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Title | Cryo-EM structure of the insect olfactory receptor OR5-Orco heterocomplex from Acyrthosiphon pisum bound with geranyl acetate | ||||||
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![]() | MEMBRANE PROTEIN | ||||||
Function / homology | ![]() olfactory receptor activity / odorant binding / signal transduction / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||
![]() | Wang, Y.D. / Qiu, L. / Guan, Z.Y. / Wang, Q. / Wang, G.R. / Yin, P. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for odorant recognition of the insect odorant receptor OR-Orco heterocomplex. Authors: Yidong Wang / Liang Qiu / Bing Wang / Zeyuan Guan / Zhi Dong / Jie Zhang / Song Cao / Lulu Yang / Bo Wang / Zhou Gong / Liwei Zhang / Weihua Ma / Zhu Liu / Delin Zhang / Guirong Wang / Ping Yin / ![]() Abstract: Insects detect and discriminate a diverse array of chemicals using odorant receptors (ORs), which are ligand-gated ion channels comprising a divergent odorant-sensing OR and a conserved odorant ...Insects detect and discriminate a diverse array of chemicals using odorant receptors (ORs), which are ligand-gated ion channels comprising a divergent odorant-sensing OR and a conserved odorant receptor co-receptor (Orco). In this work, we report structures of the OR5-Orco heterocomplex from the pea aphid alone and bound to its known activating ligand, geranyl acetate. In these structures, three Orco subunits serve as scaffold components that cannot bind the ligand and remain relatively unchanged. Upon ligand binding, the pore-forming helix S7b of OR5 shifts outward from the central pore axis, causing an asymmetrical pore opening for ion influx. Our study provides insights into odorant recognition and channel gating of the OR-Orco heterocomplex and offers structural resources to support development of innovative insecticides and repellents for pest control. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 324.1 KB | Display | ![]() |
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PDB format | ![]() | 265 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 39858MC ![]() 8z9zC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 52916.766 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | | Mass: 42454.070 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-PC1 / #4: Chemical | ChemComp-SOU / [( | Mass: 196.286 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C12H20O2 / Feature type: SUBJECT OF INVESTIGATION Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: OR-Orco heterocomplex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 8 |
Specimen | Conc.: 7.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1200 nm |
Image recording | Electron dose: 55 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
EM software | Name: cryoSPARC / Category: classification |
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CTF correction | Type: NONE |
3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 399858 / Symmetry type: POINT |