+Open data
-Basic information
Entry | Database: PDB / ID: 8v00 | |||||||||
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Title | AaegOR10 apo structure | |||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Mosquito olfactory receptor | |||||||||
Function / homology | Olfactory receptor, insect / 7tm Odorant receptor / olfactory receptor activity / odorant binding / signal transduction / identical protein binding / plasma membrane / Odorant receptor / Odorant receptor Function and homology information | |||||||||
Biological species | Aedes aegypti (yellow fever mosquito) Apocrypta bakeri (insect) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.88 Å | |||||||||
Authors | Zhao, J. / del Marmol, J. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Science / Year: 2024 Title: Structural basis of odor sensing by insect heteromeric odorant receptors. Authors: Jiawei Zhao / Andy Q Chen / Jaewook Ryu / Josefina Del Mármol / Abstract: Most insects, including human-targeting mosquitoes, detect odors through odorant-activated ion channel complexes consisting of a divergent odorant-binding subunit (OR) and a conserved co-receptor ...Most insects, including human-targeting mosquitoes, detect odors through odorant-activated ion channel complexes consisting of a divergent odorant-binding subunit (OR) and a conserved co-receptor subunit (Orco). As a basis for understanding how odorants activate these heteromeric receptors, we report here cryo-electron microscopy structures of two different heteromeric odorant receptor complexes containing ORs from disease-vector mosquitos or . These structures reveal an unexpected stoichiometry of one OR to three Orco subunits. Comparison of structures in odorant-bound and unbound states indicates that odorant binding to the sole OR subunit is sufficient to open the channel pore, suggesting a mechanism of OR activation and a conceptual framework for understanding evolution of insect odorant receptor sensitivity. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8v00.cif.gz | 724.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8v00.ent.gz | 486.4 KB | Display | PDB format |
PDBx/mmJSON format | 8v00.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8v00_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 8v00_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 8v00_validation.xml.gz | 55.4 KB | Display | |
Data in CIF | 8v00_validation.cif.gz | 83.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/8v00 ftp://data.pdbj.org/pub/pdb/validation_reports/v0/8v00 | HTTPS FTP |
-Related structure data
Related structure data | 42848MC 8v02C 8v3cC 8v3dC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 43491.168 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aedes aegypti (yellow fever mosquito) / Gene: GPRor10 / Production host: Homo sapiens (human) / References: UniProt: Q177X3 |
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#2: Protein | Mass: 53204.953 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Apocrypta bakeri (insect) / Gene: Or2 / Production host: Homo sapiens (human) / References: UniProt: B0FAQ4 |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
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Molecular weight |
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Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.21_5207 / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.88 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 386704 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.99 Å2 | ||||||||||||||||||||||||
Refine LS restraints |
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