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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | AaegOR10 apo structure | |||||||||
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![]() | Mosquito olfactory receptor / MEMBRANE PROTEIN | |||||||||
Function / homology | Olfactory receptor, insect / 7tm Odorant receptor / olfactory receptor activity / odorant binding / signal transduction / identical protein binding / plasma membrane / Odorant receptor / Odorant receptor![]() | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.88 Å | |||||||||
![]() | Zhao J / del Marmol J | |||||||||
Funding support | ![]()
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![]() | ![]() 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 (cryo-EM) structures of two different heteromeric odorant receptor complexes containing ORs from disease-vector mosquitos or . These structures reveal an unexpected stoichiometry of 1 OR to 3 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
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 46.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.6 KB 15.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.5 KB | Display | ![]() |
Images | ![]() | 181.8 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Others | ![]() ![]() | 84.5 MB 84.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 923.4 KB | Display | ![]() |
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Full document | ![]() | 923 KB | Display | |
Data in XML | ![]() | 18.1 KB | Display | |
Data in CIF | ![]() | 23 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8v00MC ![]() 8v02C ![]() 8v3cC ![]() 8v3dC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.827 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_42848_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_42848_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : AaegOR10 heterotetramer without ligand
Entire | Name: AaegOR10 heterotetramer without ligand |
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Components |
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-Supramolecule #1: AaegOR10 heterotetramer without ligand
Supramolecule | Name: AaegOR10 heterotetramer without ligand / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: Aedes aegypti OR10
Supramolecule | Name: Aedes aegypti OR10 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: Apocrypta bakeri Orco
Supramolecule | Name: Apocrypta bakeri Orco / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Odorant receptor OR10
Macromolecule | Name: Odorant receptor OR10 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 43.491168 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MASILDCPIV SVNARVWRFW SFVLKHDAMR YISIIPVTVM TFFMFTDLCR SWGNIQELII KAYFAVLYFN AVLRTLILVK DRKLYENFM QGISNVYFEI SHIDDHKIQS LLKSYTVRAR MLSISNLALG AIISTCFVVY PIFTGERGLP YGMFIPGLDS F RSPHYEII ...String: MASILDCPIV SVNARVWRFW SFVLKHDAMR YISIIPVTVM TFFMFTDLCR SWGNIQELII KAYFAVLYFN AVLRTLILVK DRKLYENFM QGISNVYFEI SHIDDHKIQS LLKSYTVRAR MLSISNLALG AIISTCFVVY PIFTGERGLP YGMFIPGLDS F RSPHYEII YIVQVVLTFP GCCMYIPFTS FFASTTLFGL VQIKTLQRQL QTFKDNINSQ DKEKVKAKVV KLIEDHKRII TY VSELNSL VTYICFVEFL SFGMMLCALL FLLNVIENHA QIVIVAAYIF MIISQIFAFY WHANEVREES MNLAEAAYSG PWV ELDNSI KKKLLLIILR AQQPLEITVG NVYPMTLEMF QSLLNASYSY FTLLRRVYN UniProtKB: Odorant receptor |
-Macromolecule #2: Odorant receptor Orco
Macromolecule | Name: Odorant receptor Orco / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 53.204953 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MKFKHQGLVA DLLPNIRVMQ GVGHFMFNYY SEGKKFPHRI YCIVTLLLLL LQYGMMAVNL MMESDDVDDL TANTITMLFF LHPIVKMIY FPVRSKIFYK TLAIWNNPNS HPLFAESNAR FHALAITKMR RLLFCVAGAT IFSVISWTGI TFIEDSVKRI T DPETNETT ...String: MKFKHQGLVA DLLPNIRVMQ GVGHFMFNYY SEGKKFPHRI YCIVTLLLLL LQYGMMAVNL MMESDDVDDL TANTITMLFF LHPIVKMIY FPVRSKIFYK TLAIWNNPNS HPLFAESNAR FHALAITKMR RLLFCVAGAT IFSVISWTGI TFIEDSVKRI T DPETNETT IIPIPRLMIR TFYPFNAMSG AGHVFALIYQ FYYLVISMAV SNSLDVLFCS WLLFACEQLQ HLKAIMKPLM EL SATLDTV VPNSGELFKA GSADHLRESQ GVQPSGNGDN VLDVDLRGIY SNRQDFTATF RPTAGTTFNG GVGPNGLTKK QEM LVRSAI KYWVERHKHV VRLVTAVGDA YGVALLLHML TTTITLTLLA YQATKVNGVN VYAATVIGYL LYTLGQVFLF CIFG NRLIE ESSSVMEAAY SCHWYDGSEE AKTFVQIVCQ QCQKAMSISG AKFFTVSLDL FASVLGAVVT YFMVLVQLK UniProtKB: Odorant receptor |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |