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Yorodumi- EMDB-49392: ELIC with propylamine facing ECD inwards in liposomes with 2:1:1 ... -
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Open data
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Basic information
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| Title | ELIC with propylamine facing ECD inwards in liposomes with 2:1:1 POPC:POPE:POPG | |||||||||
Map data | Wild Type ELIC with Propylamine facing ECD inwards in Liposomes with 2:1:1 POPC:POPE:POPG | |||||||||
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Keywords | ELIC / ion channel / pLGIC / Structural Protein / Membrane Protein / TRANSPORT PROTEIN | |||||||||
| Function / homology | Function and homology informationextracellular ligand-gated monoatomic ion channel activity / transmembrane signaling receptor activity / identical protein binding / membrane Similarity search - Function | |||||||||
| Biological species | Dickeya dadantii (bacteria) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
Authors | Dalal V / Cheng WWL | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Elife / Year: 2025Title: Cryo-EM structures of a pentameric ligand-gated ion channel in liposomes. Authors: Vikram Dalal / Brandon K Tan / Hanrui Xu / Wayland W L Cheng / ![]() Abstract: Detergents and lipid nanodiscs affect the cryo-EM structures of pentameric ligand-gated ion channels (pLGICs) including ELIC. To determine the structure of a pLGIC in a membrane environment that ...Detergents and lipid nanodiscs affect the cryo-EM structures of pentameric ligand-gated ion channels (pLGICs) including ELIC. To determine the structure of a pLGIC in a membrane environment that supports ion channel function, we performed single particle cryo-EM of ELIC in liposomes. ELIC activation and desensitization were confirmed in liposomes with a stopped-flow thallium flux assay. Using WT ELIC and a non-desensitizing mutant (ELIC5), we captured resting, activated, and desensitized structures at high resolution. In the desensitized structure, the ion conduction pore has a constriction at the 9' leucine of the pore-lining M2 helix, indicating that 9' is the desensitization gate in ELIC. The agonist-bound structures of ELIC in liposomes are distinct from those in nanodiscs. In general, the transmembrane domain is more loosely packed in liposomes compared to nanodiscs. It has been suggested that large nanodiscs are superior for supporting membrane protein function. However, ELIC localizes to the rim of large circularized nanodiscs, and structures of ELIC in large nanodiscs deviate from the liposome structures more than those in small nanodiscs. Using liposomes for cryo-EM structure determination of a pLGIC increases our confidence that the structures are snapshots of functional states. #1: Journal: Elife / Year: 2025Title: Cryo-EM structures of a pentameric ligand-gated ion channel in liposomes Authors: Dalal V / Tan BK / Xu H / Cheng WW | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_49392.map.gz | 59.7 MB | EMDB map data format | |
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| Header (meta data) | emd-49392-v30.xml emd-49392.xml | 21.4 KB 21.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_49392_fsc.xml | 9.2 KB | Display | FSC data file |
| Images | emd_49392.png | 55 KB | ||
| Filedesc metadata | emd-49392.cif.gz | 6.1 KB | ||
| Others | emd_49392_additional_1.map.gz emd_49392_half_map_1.map.gz emd_49392_half_map_2.map.gz | 58.7 MB 49.6 MB 49.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-49392 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-49392 | HTTPS FTP |
-Validation report
| Summary document | emd_49392_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_49392_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_49392_validation.xml.gz | 15.8 KB | Display | |
| Data in CIF | emd_49392_validation.cif.gz | 21.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49392 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49392 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ngsMC ![]() 9ngcC ![]() 9ngfC ![]() 9nggC ![]() 9ngiC ![]() 9ngqC ![]() 9ngrC ![]() 9nh4C 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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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_49392.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Wild Type ELIC with Propylamine facing ECD inwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.865 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Wild Type ELIC with Propylamine facing ECD inwards...
| File | emd_49392_additional_1.map | ||||||||||||
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| Annotation | Wild Type ELIC with Propylamine facing ECD inwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Wild Type ELIC with Propylamine facing ECD inwards...
| File | emd_49392_half_map_1.map | ||||||||||||
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| Annotation | Wild Type ELIC with Propylamine facing ECD inwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Wild Type ELIC with Propylamine facing ECD inwards...
| File | emd_49392_half_map_2.map | ||||||||||||
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| Annotation | Wild Type ELIC with Propylamine facing ECD inwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : ELIC with propylamine facing ECD inwards in liposomes with 2:1:1 ...
| Entire | Name: ELIC with propylamine facing ECD inwards in liposomes with 2:1:1 POPC:POPE:POPG |
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| Components |
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-Supramolecule #1: ELIC with propylamine facing ECD inwards in liposomes with 2:1:1 ...
| Supramolecule | Name: ELIC with propylamine facing ECD inwards in liposomes with 2:1:1 POPC:POPE:POPG type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Dickeya dadantii (bacteria) |
-Macromolecule #1: Erwinia chrysanthemi ligand-gated ion channel
| Macromolecule | Name: Erwinia chrysanthemi ligand-gated ion channel / type: protein_or_peptide / ID: 1 / Number of copies: 5 / Enantiomer: LEVO |
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| Source (natural) | Organism: Dickeya dadantii (bacteria) |
| Molecular weight | Theoretical: 36.879 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: APADNAADAR PVDVSVSIFI NKIYGVNTLE QTYKVDGYIV AQWTGKPRKT PGDKPLIVEN TQIERWINNG LWVPALEFIN VVGSPDTGN KRLMLFPDGR VIYNARFLGS FSNDMDFRLF PFDRQQFVLE LEPFSYNNQQ LRFSDIQVYT ENIDNEEIDE W WIRGKAST ...String: APADNAADAR PVDVSVSIFI NKIYGVNTLE QTYKVDGYIV AQWTGKPRKT PGDKPLIVEN TQIERWINNG LWVPALEFIN VVGSPDTGN KRLMLFPDGR VIYNARFLGS FSNDMDFRLF PFDRQQFVLE LEPFSYNNQQ LRFSDIQVYT ENIDNEEIDE W WIRGKAST HISDIRYDHL SSVQPNQNEF SRITVRIDAV RNPSYYLWSF ILPLGLIIAA SWSVFWLESF SERLQTSFTL ML TVVAYAF YTSNILPRLP YTTVIDQMII AGYGSIFAAI LLIIFAHHRQ ANGVEDDLLI QRCRLAFPLG FLAIGCVLVI RGI TL UniProtKB: Gamma-aminobutyric-acid receptor subunit beta-1 |
-Macromolecule #2: 3-AMINOPROPANE
| Macromolecule | Name: 3-AMINOPROPANE / type: ligand / ID: 2 / Number of copies: 5 / Formula: 3CN |
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| Molecular weight | Theoretical: 59.11 Da |
| Chemical component information | ![]() ChemComp-3CN: |
-Macromolecule #3: SODIUM ION
| Macromolecule | Name: SODIUM ION / type: ligand / ID: 3 / Number of copies: 4 |
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| Molecular weight | Theoretical: 22.99 Da |
-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 |
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| Grid | Model: Quantifoil R2/2 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Spherical aberration corrector: Cs Corrected System |
| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Average exposure time: 7.27 sec. / Average electron dose: 54.4 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Calibrated magnification: 75000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 75000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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| Output model | ![]() PDB-9ngs: |
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About Yorodumi



Keywords
Dickeya dadantii (bacteria)
Authors
United States, 2 items
Citation
















Z (Sec.)
Y (Row.)
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FIELD EMISSION GUN


