+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-35821 | |||||||||
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Title | Human neuronal gap junction channel connexin 36 | |||||||||
Map data | ||||||||||
Sample |
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Keywords | channel neuronal connexin dodecamer / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information Electric 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 / Resolution: 2.69 Å | |||||||||
Authors | Mao WX / Chen SS | |||||||||
Funding support | China, 1 items
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Citation | Journal: Arch Biochem Biophys / Year: 2024 Title: Assembly mechanisms of the neuronal gap junction channel connexin 36 elucidated by Cryo-EM. Authors: Wenxuan Mao / Shanshuang Chen / Abstract: Electrical synapses are essential components of neural circuits. Neuronal signal transduction across electrical synapses is primarily mediated by gap junction channels composed of Connexin36 (Cx36), ...Electrical synapses are essential components of neural circuits. Neuronal signal transduction across electrical synapses is primarily mediated by gap junction channels composed of Connexin36 (Cx36), the lack of which causes impaired electrical coupling between certain neurons including cortical interneurons and thalamic reticular nucleus (TRN) neurons. However, the structural basis underlying Cx36 function and assembly remains elusive. Recently, Lee et al. reported cryo-EM structures of Cx36, thus provided first insights of its gating mechanism. Here, we report a consistent cryo-EM structure of Cx36 determined in parallel, and describe unique interactions underpinning its assembly mechanism in complementary to the competing work. In particular, we found non-canonical electrostatic interactions between protomers from opposing hemichannels and a steric complementary site between adjacent protomers within a hemichannel, which together provide a structural explanation for the assembly specificity in homomeric and heteromeric gap junction channels. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_35821.map.gz | 41.9 MB | EMDB map data format | |
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Header (meta data) | emd-35821-v30.xml emd-35821.xml | 13.3 KB 13.3 KB | Display Display | EMDB header |
Images | emd_35821.png | 55.1 KB | ||
Filedesc metadata | emd-35821.cif.gz | 5.1 KB | ||
Others | emd_35821_half_map_1.map.gz emd_35821_half_map_2.map.gz | 77.6 MB 77.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-35821 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-35821 | HTTPS FTP |
-Related structure data
Related structure data | 8iygMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_35821.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_35821_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_35821_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : human neuronal gap junction channel connexin 36
Entire | Name: human neuronal gap junction channel connexin 36 |
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Components |
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-Supramolecule #1: human neuronal gap junction channel connexin 36
Supramolecule | Name: human neuronal gap junction channel connexin 36 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Gap junction delta-2 protein
Macromolecule | Name: Gap junction delta-2 protein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 36.135672 KDa |
Recombinant expression | Organism: eukaryotic plasmids (others) |
Sequence | String: MGEWTILERL LEAAVQQHST MIGRILLTVV VIFRILIVAI VGETVYDDEQ TMFVCNTLQP GCNQACYDRA FPISHIRYWV FQIIMVCTP SLCFITYSVH QSAKQRERRY STVFLALDRD PPESIGGPGG TGGGGSGGGK REDKKLQNAI VNGVLQNTEN T SKETEPDC ...String: MGEWTILERL LEAAVQQHST MIGRILLTVV VIFRILIVAI VGETVYDDEQ TMFVCNTLQP GCNQACYDRA FPISHIRYWV FQIIMVCTP SLCFITYSVH QSAKQRERRY STVFLALDRD PPESIGGPGG TGGGGSGGGK REDKKLQNAI VNGVLQNTEN T SKETEPDC LEVKELTPHP SGLRTASKSK LRRQEGISRF YIIQVVFRNA LEIGFLVGQY FLYGFSVPGL YECNRYPCIK EV ECYVSRP TEKTVFLVFM FAVSGICVVL NLAELNHLGW RKIKLAVRGA QAKRKSIYEI RNKDLPRVSV PNFGRTQSSD SAY V UniProtKB: Gap junction delta-2 protein |
-Macromolecule #2: CHOLESTEROL HEMISUCCINATE
Macromolecule | Name: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 2 / Number of copies: 48 / Formula: Y01 |
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Molecular weight | Theoretical: 486.726 Da |
Chemical component information | ChemComp-Y01: |
-Macromolecule #3: DODECYL-BETA-D-MALTOSIDE
Macromolecule | Name: DODECYL-BETA-D-MALTOSIDE / type: ligand / ID: 3 / Number of copies: 84 / Formula: LMT |
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Molecular weight | Theoretical: 510.615 Da |
Chemical component information | ChemComp-LMT: |
-Experimental details
-Structure determination
Processing | single particle reconstruction |
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Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 1.56 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Initial angle assignment | Type: OTHER |
Final angle assignment | Type: OTHER |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.69 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 117469 |