7Z22
Connexin43 gap junction channel structure in nanodisc
Summary for 7Z22
| Entry DOI | 10.2210/pdb7z22/pdb |
| Related | 7Z1T |
| EMDB information | 14455 |
| Descriptor | Gap junction alpha-1 protein (1 entity in total) |
| Functional Keywords | gap junction channel, connexin, cell communication, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 12 |
| Total formula weight | 516736.03 |
| Authors | Qi, C.,Korkhov, M.V. (deposition date: 2022-02-25, release date: 2023-03-08, Last modification date: 2024-10-16) |
| Primary citation | Qi, 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: 37535063DOI: 10.7554/eLife.87616 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.95 Å) |
Structure validation
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