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7Z1T

Connexin43 gap junction channel structure in digitonin

Summary for 7Z1T
Entry DOI10.2210/pdb7z1t/pdb
EMDB information14452
DescriptorGap junction alpha-1 protein (1 entity in total)
Functional Keywordsgap junction channel, connexin, cell communication, membrane protein
Biological sourceHomo sapiens (human)
Total number of polymer chains12
Total formula weight516736.03
Authors
Qi, C.,Korkhov, M.V. (deposition date: 2022-02-25, release date: 2023-03-08, Last modification date: 2024-11-13)
Primary citationQi, C.,Acosta Gutierrez, S.,Lavriha, P.,Othman, A.,Lopez-Pigozzi, D.,Bayraktar, E.,Schuster, D.,Picotti, P.,Zamboni, N.,Bortolozzi, M.,Gervasio, F.L.,Korkhov, V.M.
Structure of the connexin-43 gap junction channel in a putative closed state.
Elife, 12:-, 2023
Cited by
PubMed Abstract: Gap junction channels (GJCs) mediate intercellular communication by connecting two neighbouring cells and enabling direct exchange of ions and small molecules. Cell coupling via connexin-43 (Cx43) GJCs is important in a wide range of cellular processes in health and disease (Churko and Laird, 2013; Liang et al., 2020; Poelzing and Rosenbaum, 2004), yet the structural basis of Cx43 function and regulation has not been determined until now. Here, we describe the structure of a human Cx43 GJC solved by cryo-EM and single particle analysis at 2.26 Å resolution. The pore region of Cx43 GJC features several lipid-like densities per Cx43 monomer, located close to a putative lateral access site at the monomer boundary. We found a previously undescribed conformation on the cytosolic side of the pore, formed by the N-terminal domain and the transmembrane helix 2 of Cx43 and stabilized by a small molecule. Structures of the Cx43 GJC and hemichannels (HCs) in nanodiscs reveal a similar gate arrangement. The features of the Cx43 GJC and HC cryo-EM maps and the channel properties revealed by molecular dynamics simulations suggest that the captured states of Cx43 are consistent with a closed state.
PubMed: 37535063
DOI: 10.7554/eLife.87616
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.26 Å)
Structure validation

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