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Yorodumi- EMDB-60763: Consensus map of Cx36/GJD2 gap junction intercellular channel in ... -
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Basic information
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| Title | Consensus map of Cx36/GJD2 gap junction intercellular channel in soybean polar lipid nanodiscs, treated with a 10-fold molar excess of carbenoxolone and incubated shortly (including D6 and D1 symmetry maps) | ||||||||||||
Map data | primary map refined with D6 symmetry | ||||||||||||
Sample |
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Keywords | Gap junction / Connexin36 / Inhibitor / Carbenoxolone / MEMBRANE PROTEIN | ||||||||||||
| Function / homology | Function and homology informationElectric Transmission Across Gap Junctions / connexin complex / Gap junction assembly / gap junction channel activity / neuronal action potential / visual perception / cell-cell signaling / chemical synaptic transmission / synapse / plasma membrane Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.04 Å | ||||||||||||
Authors | Jang HS | ||||||||||||
| Funding support | Korea, Republic Of, 3 items
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Citation | Journal: To Be PublishedTitle: Structural insights into the closing mechanism of gap junction intercellular channels by carbenoxolone Authors: Lee CW / Jang HS / Woo JS | ||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_60763.map.gz | 213 MB | EMDB map data format | |
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| Header (meta data) | emd-60763-v30.xml emd-60763.xml | 21.5 KB 21.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_60763_fsc.xml | 17.8 KB | Display | FSC data file |
| Images | emd_60763.png | 87 KB | ||
| Filedesc metadata | emd-60763.cif.gz | 5.9 KB | ||
| Others | emd_60763_additional_1.map.gz emd_60763_half_map_1.map.gz emd_60763_half_map_2.map.gz | 212.4 MB 391.6 MB 391.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-60763 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-60763 | HTTPS FTP |
-Validation report
| Summary document | emd_60763_validation.pdf.gz | 857.2 KB | Display | EMDB validaton report |
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| Full document | emd_60763_full_validation.pdf.gz | 856.7 KB | Display | |
| Data in XML | emd_60763_validation.xml.gz | 25.2 KB | Display | |
| Data in CIF | emd_60763_validation.cif.gz | 33 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60763 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60763 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9inzC ![]() 9ip5C ![]() 9ipmC ![]() 9ipnC ![]() 9ipoC 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_60763.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | primary map refined with D6 symmetry | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.81 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: the map refined with D1 symmetry, using same particles to D6 map
| File | emd_60763_additional_1.map | ||||||||||||
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| Annotation | the map refined with D1 symmetry, using same particles to D6 map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: half-map of primary map
| File | emd_60763_half_map_1.map | ||||||||||||
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| Annotation | half-map of primary map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: half-map of primary map
| File | emd_60763_half_map_2.map | ||||||||||||
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| Annotation | half-map of primary map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Connexin36
| Entire | Name: Connexin36 |
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| Components |
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-Supramolecule #1: Connexin36
| Supramolecule | Name: Connexin36 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: BRIL-fused connexin36 gap junction intercellular channel is reconstituted into lipid nanodiscs with soybean polar lipids and MSP1E1. Carbenoxolone dissolved in 10% (v/v) DMSO is treated to ...Details: BRIL-fused connexin36 gap junction intercellular channel is reconstituted into lipid nanodiscs with soybean polar lipids and MSP1E1. Carbenoxolone dissolved in 10% (v/v) DMSO is treated to the sample with 10-fold molar excess to Cx36 protomer. Sample was incubated for 1 min before grid loading. |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Connexin36
| Macromolecule | Name: Connexin36 / type: protein_or_peptide / ID: 1 Details: The human Cx36-BRIL proteins were expressed as fusion constructs with a human rhinovirus (HRV) 3C cleavage site, an enhanced yellow fluorescence protein (eYFP) tag, a 10xHis-tag and a rho- ...Details: The human Cx36-BRIL proteins were expressed as fusion constructs with a human rhinovirus (HRV) 3C cleavage site, an enhanced yellow fluorescence protein (eYFP) tag, a 10xHis-tag and a rho-1D4 epitope tag (8 amino acid sequence of TETSQVAPA) at its C-terminus. Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MGEWTILERL LEAAVQQHST MIGRILLTV VVIFRILIVA I VGETVYDD EQTMFVCNTL QP GCNQACY DRAFPISHIR YWV FQIIMV CTPSLCFITY SVHQ SAKQR ERRADLEDNW ETLND NLKV IEKADNAAQV KDALTK MRA AALDAQKATP PKLEDKS PD ...String: MGEWTILERL LEAAVQQHST MIGRILLTV VVIFRILIVA I VGETVYDD EQTMFVCNTL QP GCNQACY DRAFPISHIR YWV FQIIMV CTPSLCFITY SVHQ SAKQR ERRADLEDNW ETLND NLKV IEKADNAAQV KDALTK MRA AALDAQKATP PKLEDKS PD SPEMKDFRHG FDILVGQI D DALKLANEGK VKEAQAAAE QLKTTRNAYI QKYLKLRRQE GISRFYIIQ VVFRNALEIG F LVGQYFLY GFSVPGLYEC NR YPCIKEV ECYVSRPTEK TVF LVFMFA VSGICVVLNL AELN HLGWR KIKLAVRGAQ AKRKS IYEI RNKDLPRVSV PNFGRT QSS DSAYVSRGDM LEVLFQ UniProtKB: Gap junction delta-2 protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 3.0 mg/mL | ||||||||||||
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| Buffer | pH: 7.5 Component:
Details: 20mM HEPES(pH 7.5), 150mM KCl, 2mM beta-mercaptoethanol | ||||||||||||
| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: OTHER | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number real images: 5001 / Average exposure time: 6.79 sec. / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.25 µm / Nominal defocus min: 0.75 µm / Nominal magnification: 96000 |
| Sample stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
Korea, Republic Of, 3 items
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Processing
FIELD EMISSION GUN

