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- EMDB-33274: Human Cx36/GJD2 (N-terminal deletion mutant) gap junction channel... -
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Open data
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Basic information
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Title | Human Cx36/GJD2 (N-terminal deletion mutant) gap junction channel in soybean lipids (D6 symmetry) | |||||||||
![]() | sharpened map | |||||||||
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![]() | Connexin 36 / Cx36 / Gap Junction Channel / GJD2 / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() 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 | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
![]() | Lee SN / Cho HJ / Jeong H / Ryu B / Lee HJ / Lee HH / Woo JS | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel. Authors: Seu-Na Lee / Hwa-Jin Cho / Hyeongseop Jeong / Bumhan Ryu / Hyuk-Joon Lee / Minsoo Kim / Jejoong Yoo / Jae-Sung Woo / Hyung Ho Lee / ![]() Abstract: Connexin 36 (Cx36) is responsible for signal transmission in electrical synapses by forming interneuronal gap junctions. Despite the critical role of Cx36 in normal brain function, the molecular ...Connexin 36 (Cx36) is responsible for signal transmission in electrical synapses by forming interneuronal gap junctions. Despite the critical role of Cx36 in normal brain function, the molecular architecture of the Cx36 gap junction channel (GJC) is unknown. Here, we determine cryo-electron microscopy structures of Cx36 GJC at 2.2-3.6 Å resolutions, revealing a dynamic equilibrium between its closed and open states. In the closed state, channel pores are obstructed by lipids, while N-terminal helices (NTHs) are excluded from the pore. In the open state with pore-lining NTHs, the pore is more acidic than those in Cx26 and Cx46/50 GJCs, explaining its strong cation selectivity. The conformational change during channel opening also includes the α-to-π-helix transition of the first transmembrane helix, which weakens the protomer-protomer interaction. Our structural analyses provide high resolution information on the conformational flexibility of Cx36 GJC and suggest a potential role of lipids in the channel gating. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 168 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.4 KB 14.4 KB | Display Display | ![]() |
Images | ![]() | 129.5 KB | ||
Others | ![]() ![]() | 165.3 MB 165.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7xl8MC ![]() 7xkiC ![]() 7xkkC ![]() 7xktC ![]() 7xnhC ![]() 7xnvC ![]() 8hkpC C: citing same article ( M: atomic model generated by this map |
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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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Annotation | sharpened map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.8415 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: half map B
File | emd_33274_half_map_1.map | ||||||||||||
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Annotation | half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map A
File | emd_33274_half_map_2.map | ||||||||||||
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Annotation | half map A | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Cx36-delN8
Entire | Name: Cx36-delN8 |
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Components |
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-Supramolecule #1: Cx36-delN8
Supramolecule | Name: Cx36-delN8 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-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: ![]() |
Molecular weight | Theoretical: 36.584242 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRLLEAAVQQ HSTMIGRILL TVVVIFRILI VAIVGETVYD DEQTMFVCNT LQPGCNQACY DRAFPISHIR YWVFQIIMVC TPSLCFITY SVHQSAKQRE RRYSTVFLAL DRDPPESIGG PGGTGGGGSG GGKREDKKLQ NAIVNGVLQN TENTSKETEP D CLEVKELT ...String: MRLLEAAVQQ HSTMIGRILL TVVVIFRILI VAIVGETVYD DEQTMFVCNT LQPGCNQACY DRAFPISHIR YWVFQIIMVC TPSLCFITY SVHQSAKQRE RRYSTVFLAL DRDPPESIGG PGGTGGGGSG GGKREDKKLQ NAIVNGVLQN TENTSKETEP D CLEVKELT PHPSGLRTAS KSKLRRQEGI SRFYIIQVVF RNALEIGFLV GQYFLYGFSV PGLYECNRYP CIKEVECYVS RP TEKTVFL VFMFAVSGIC VVLNLAELNH LGWRKIKLAV RGAQAKRKSI YEIRNKDLPR VSVPNFGRTQ SSDSAYVSRG DML EVLFQ UniProtKB: Gap junction delta-2 protein |
-Macromolecule #2: 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE
Macromolecule | Name: 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE / type: ligand / ID: 2 / Number of copies: 84 / Formula: MC3 |
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Molecular weight | Theoretical: 677.933 Da |
Chemical component information | ![]() ChemComp-MC3: |
-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 BIOQUANTUM (6k x 4k) / Average electron dose: 61.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.9 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 460806 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |