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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | AgamOR28 structure without ligand | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Mosquitoes / Olfaction / Channel / Heterotetramer / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationolfactory receptor activity / detection of chemical stimulus involved in sensory perception of smell / odorant binding / signal transduction / identical protein binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() Apocrypta bakeri (insect) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.62 Å | |||||||||
Authors | Zhao J / del Marmol J | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Science / Year: 2024Title: 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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_42945.map.gz | 27.4 MB | EMDB map data format | |
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| Header (meta data) | emd-42945-v30.xml emd-42945.xml | 15.8 KB 15.8 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_42945_fsc.xml | 7.9 KB | Display | FSC data file |
| Images | emd_42945.png | 155 KB | ||
| Filedesc metadata | emd-42945.cif.gz | 5.8 KB | ||
| Others | emd_42945_half_map_1.map.gz emd_42945_half_map_2.map.gz | 48.9 MB 48.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-42945 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-42945 | HTTPS FTP |
-Validation report
| Summary document | emd_42945_validation.pdf.gz | 935.7 KB | Display | EMDB validaton report |
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| Full document | emd_42945_full_validation.pdf.gz | 935.3 KB | Display | |
| Data in XML | emd_42945_validation.xml.gz | 15.4 KB | Display | |
| Data in CIF | emd_42945_validation.cif.gz | 20.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42945 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42945 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8v3cMC ![]() 8v00C ![]() 8v02C ![]() 8v3dC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_42945.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_42945_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_42945_half_map_2.map | ||||||||||||
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Sample components
-Entire : AgamOR28 heterotetramer without ligand
| Entire | Name: AgamOR28 heterotetramer without ligand |
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| Components |
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-Supramolecule #1: AgamOR28 heterotetramer without ligand
| Supramolecule | Name: AgamOR28 heterotetramer without ligand / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: Anopheles gambiae OR28
| Supramolecule | Name: Anopheles gambiae OR28 / 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: Apocrypta bakeri (insect) |
-Macromolecule #1: OR28
| Macromolecule | Name: OR28 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 45.826898 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MARLVLHEVR YVLMAMLYIS RGMAKQIQNS TIDLYVYWFL TFIPIASLCV PQFTYLVVDT KSLIDFISVL VPITEILLTN GKMIICNVK RGKIINLINQ VQVAWDECAK SEHLEIQTLI TATAKKTKIF VIIYTTSFLL ICVEYSSMPL FKLIYHSAVY G KQSNYTIA ...String: MARLVLHEVR YVLMAMLYIS RGMAKQIQNS TIDLYVYWFL TFIPIASLCV PQFTYLVVDT KSLIDFISVL VPITEILLTN GKMIICNVK RGKIINLINQ VQVAWDECAK SEHLEIQTLI TATAKKTKIF VIIYTTSFLL ICVEYSSMPL FKLIYHSAVY G KQSNYTIA LPYLSRFAYS TESTTSFAWT YFFILLGVYL LALTLSGFDS LFATLVMHVK MMFKVLKFEI EQLGLDLSAG KS HVELQAK LKQIILKHKT NLSLIEQLED GFSFFLMAQF LTSSILVCVV LYELTMVFGW NEDTFKTVTY LPGAILQLFL FCW YAQQIT EEARLVSDHI YNIPWYLADP KLQKDILTFM VKAQKPTGVT ASKFYMVTLQ TFQRISSTSY SYFTLLQTIN QQ UniProtKB: Uncharacterized protein |
-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: Apocrypta bakeri (insect) |
| Molecular weight | Theoretical: 53.204953 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| 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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Processing | 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: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| 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 |
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About Yorodumi




Keywords
Authors
United States, 2 items
Citation






Z (Sec.)
Y (Row.)
X (Col.)




































Homo sapiens (human)
Processing
FIELD EMISSION GUN

