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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | AgamOR28 structure bound to 2,4,5-trimethylthiazole | |||||||||
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![]() | Mosquito olfactory receptor / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() olfactory 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 | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.95 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 | ![]() | 49.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16 KB 16 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 7.9 KB | Display | ![]() |
Images | ![]() | 138.5 KB | ||
Filedesc metadata | ![]() | 6 KB | ||
Others | ![]() ![]() | 49 MB 49 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 897 KB | Display | ![]() |
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Full document | ![]() | 896.7 KB | Display | |
Data in XML | ![]() | 15.4 KB | Display | |
Data in CIF | ![]() | 20.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8v3dMC ![]() 8v00C ![]() 8v02C ![]() 8v3cC 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: 1.061 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_42946_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_42946_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : AgamOR28 heterotetramer bound to 2,4,5-trimethylthiazole
Entire | Name: AgamOR28 heterotetramer bound to 2,4,5-trimethylthiazole |
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Components |
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-Supramolecule #1: AgamOR28 heterotetramer bound to 2,4,5-trimethylthiazole
Supramolecule | Name: AgamOR28 heterotetramer bound to 2,4,5-trimethylthiazole type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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-Supramolecule #2: Anopheles gambiae OR28
Supramolecule | Name: Anopheles gambiae OR28 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #2 |
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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: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Odorant receptor Orco
Macromolecule | Name: Odorant receptor Orco / type: protein_or_peptide / ID: 1 / 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 |
-Macromolecule #2: OR28
Macromolecule | Name: OR28 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 45.826898 KDa |
Recombinant expression | Organism: ![]() |
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 #3: 2,4,5-trimethyl-1,3-thiazole
Macromolecule | Name: 2,4,5-trimethyl-1,3-thiazole / type: ligand / ID: 3 / Number of copies: 1 / Formula: A1AFC |
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Molecular weight | Theoretical: 127.207 Da |
-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: 50.0 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 |