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Yorodumi- EMDB-49383: ELIC facing ECD outwards in liposomes with 2:1:1 POPC:POPE:POPG -
+ Open data
Open data
- Basic information
Basic information
| Entry |  | |||||||||
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| Title | ELIC facing ECD outwards in liposomes with 2:1:1 POPC:POPE:POPG | |||||||||
|  Map data | Apo Wild Type ELIC facing ECD outwards in Liposomes with 2:1:1 POPC:POPE:POPG | |||||||||
|  Sample | 
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|  Keywords | ELIC / ion channel / pLGIC / Structural Protein / Membrane Protein / TRANSPORT PROTEIN | |||||||||
| Function / homology |  Function and homology information extracellular 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: 3.4 Å | |||||||||
|  Authors | Dalal V / Cheng WWL | |||||||||
| Funding support |  United States, 2 items 
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|  Citation |  Journal: Elife / Year: 2025 Title: 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: 2025 Title: Cryo-EM structures of a pentameric ligand-gated ion channel in liposomes Authors: Dalal V / Tan BK / Xu H / Cheng WW | |||||||||
| History | 
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- Structure visualization
Structure visualization
| Supplemental images | 
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- Downloads & links
Downloads & links
-EMDB archive
| Map data |  emd_49383.map.gz | 59.9 MB |  EMDB map data format | |
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| Header (meta data) |  emd-49383-v30.xml  emd-49383.xml | 20.9 KB 20.9 KB | Display Display |  EMDB header | 
| FSC (resolution estimation) |  emd_49383_fsc.xml | 9.2 KB | Display |  FSC data file | 
| Images |  emd_49383.png | 66 KB | ||
| Filedesc metadata |  emd-49383.cif.gz | 6.1 KB | ||
| Others |  emd_49383_additional_1.map.gz  emd_49383_half_map_1.map.gz  emd_49383_half_map_2.map.gz | 58.6 MB 49.5 MB 49.5 MB | ||
| Archive directory |  http://ftp.pdbj.org/pub/emdb/structures/EMD-49383  ftp://ftp.pdbj.org/pub/emdb/structures/EMD-49383 | HTTPS FTP | 
-Validation report
| Summary document |  emd_49383_validation.pdf.gz | 962.2 KB | Display |  EMDB validaton report | 
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| Full document |  emd_49383_full_validation.pdf.gz | 961.7 KB | Display | |
| Data in XML |  emd_49383_validation.xml.gz | 14.7 KB | Display | |
| Data in CIF |  emd_49383_validation.cif.gz | 21.1 KB | Display | |
| Arichive directory |  https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49383  ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-49383 | HTTPS FTP | 
-Related structure data
| Related structure data |  9ngfMC  9ngcC  9nggC  9ngiC  9ngqC  9ngrC  9ngsC  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 | 
- Links
Links
| EMDB pages |  EMDB (EBI/PDBe) /  EMDataResource | 
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| Related items in Molecule of the Month | 
- Map
Map
| File |  Download / File: emd_49383.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Apo Wild Type ELIC facing ECD outwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
 
 Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.868 Å | ||||||||||||||||||||||||||||||||||||
| Density | 
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML: 
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-Supplemental data
-Additional map: Apo Wild Type ELIC facing ECD outwards in...
| File | emd_49383_additional_1.map | ||||||||||||
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| Annotation | Apo Wild Type ELIC facing ECD outwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||
| Projections & Slices | 
 | ||||||||||||
| Density Histograms | 
-Half map: Apo Wild Type ELIC facing ECD outwards in...
| File | emd_49383_half_map_1.map | ||||||||||||
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| Annotation | Apo Wild Type ELIC facing ECD outwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||
| Projections & Slices | 
 | ||||||||||||
| Density Histograms | 
-Half map: Apo Wild Type ELIC facing ECD outwards in...
| File | emd_49383_half_map_2.map | ||||||||||||
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| Annotation | Apo Wild Type ELIC facing ECD outwards in Liposomes with 2:1:1 POPC:POPE:POPG | ||||||||||||
| Projections & Slices | 
 | ||||||||||||
| Density Histograms | 
- Sample components
Sample components
-Entire : ELIC facing ECD outwards in liposomes with 2:1:1 POPC:POPE:POPG
| Entire | Name: ELIC facing ECD outwards in liposomes with 2:1:1 POPC:POPE:POPG | 
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| Components | 
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-Supramolecule #1: ELIC facing ECD outwards in liposomes with 2:1:1 POPC:POPE:POPG
| Supramolecule | Name: ELIC facing ECD outwards 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:   Escherichia coli (E. coli) | 
| 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: SODIUM ION
| Macromolecule | Name: SODIUM ION / type: ligand / ID: 2 / Number of copies: 5 | 
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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 | 
- Sample preparation
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 | 
- Electron microscopy
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 electron dose: 55.4 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 | 
+ Image processing
Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: AB INITIO MODEL | 
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| Output model |  PDB-9ngf:  | 
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