Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 1347, Year 2023
Publish date	Mar 11, 2023
Authors	Seu-Na Lee / Hwa-Jin Cho / Hyeongseop Jeong / Bumhan Ryu / Hyuk-Joon Lee / Minsoo Kim / Jejoong Yoo / Jae-Sung Woo / Hyung Ho Lee /
PubMed 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.
External links	Nat Commun / PubMed:36906653 / PubMed Central
Methods	EM (single particle)
Resolution	2.2 - 7.2 Å
Structure data	33254 7xki EMDB-33254, PDB-7xki: Human Cx36/GJD2 (N-terminal deletion BRIL-fused mutant) gap junction channel in soybean lipids (D6 symmetry) Method: EM (single particle) / Resolution: 3.4 Å EMDB-33255: Human Cx36/GJD2 (N-terminal deletion BRIL-fused mutant) gap junction channel in soybean lipids (C1 symmetry) Method: EM (single particle) / Resolution: 4.5 Å 33256 7xkk EMDB-33256, PDB-7xkk: Human Cx36/GJD2 gap junction channel in detergents Method: EM (single particle) / Resolution: 3.2 Å 33270 7xkt EMDB-33270, PDB-7xkt: Human Cx36/GJD2 (BRIL-fused mutant) gap junction channel in detergents at 2.2 Angstroms resolution Method: EM (single particle) / Resolution: 2.2 Å 33274 7xl8 EMDB-33274, PDB-7xl8: Human Cx36/GJD2 (N-terminal deletion mutant) gap junction channel in soybean lipids (D6 symmetry) Method: EM (single particle) / Resolution: 3.0 Å EMDB-33275: Human Cx36/GJD2 (N-terminal deletion mutant) gap junction channel in soybean lipids (C1 symmetry) Method: EM (single particle) / Resolution: 3.41 Å 33315 7xnh EMDB-33315, PDB-7xnh: Human Cx36/GJD2 gap junction channel with pore-lining N-terminal helices in soybean lipids Method: EM (single particle) / Resolution: 3.1 Å 33327 7xnv EMDB-33327, PDB-7xnv: Structurally hetero-junctional human Cx36/GJD2 gap junction channel in soybean lipids (C6 symmetry) Method: EM (single particle) / Resolution: 3.4 Å EMDB-33328: Structurally hetero-junctional human Cx36/GJD2 gap junction channel in soybean lipids (C1 symmetry) Method: EM (single particle) / Resolution: 4.9 Å EMDB-34822: Human Cx36/GJD2 (BRIL-fused mutant) gap junction channel in soybean lipids Method: EM (single particle) / Resolution: 3.4 Å 34856 8hkp EMDB-34856, PDB-8hkp: Structurally hetero-junctional human Cx36/GJD2 gap junction channel in detergents (C6 symmetry) Method: EM (single particle) / Resolution: 3.6 Å EMDB-34857: Structurally hetero-junctional human Cx36/GJD2 gap junction channel in detergents (C1 symmetry) Method: EM (single particle) / Resolution: 7.2 Å
Chemicals	ChemComp-MC3: 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM ChemComp-Y01: CHOLESTEROL HEMISUCCINATE ChemComp-LHG: 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipidYM / Phosphatidylglycerol ChemComp-HOH: WATER / Water ChemComp-AV0: Lauryl Maltose Neopentyl Glycol
Source	homo sapiens (human) escherichia coli (E. coli)
Keywords	MEMBRANE PROTEIN / connexin 36 / Gap Junction Channel / Cx36 / GJD2 / BRIL