8UIP
Cryo-EM Structure of Human Ninjurin1 curved oligomer
Summary for 8UIP
| Entry DOI | 10.2210/pdb8uip/pdb |
| EMDB information | 42301 |
| Descriptor | Ninjurin-1 (1 entity in total) |
| Functional Keywords | ninjurin1, ninj1, inflammation, inflammasome, pyroptosis, plasma membrane rupture, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 49070.99 |
| Authors | |
| Primary citation | David, L.,Borges, J.P.,Hollingsworth, L.R.,Volchuk, A.,Jansen, I.,Garlick, E.,Steinberg, B.E.,Wu, H. NINJ1 mediates plasma membrane rupture by cutting and releasing membrane disks. Cell, 187:2224-2235.e16, 2024 Cited by PubMed Abstract: The membrane protein NINJ1 mediates plasma membrane rupture in pyroptosis and other lytic cell death pathways. Here, we report the cryo-EM structure of a NINJ1 oligomer segmented from NINJ1 rings. Each NINJ1 subunit comprises amphipathic (⍺1, ⍺2) and transmembrane (TM) helices (⍺3, ⍺4) and forms a chain of subunits, mainly by the TM helices and ⍺1. ⍺3 and ⍺4 are kinked, and the Gly residues are important for function. The NINJ1 oligomer possesses a concave hydrophobic side that should face the membrane and a convex hydrophilic side formed by ⍺1 and ⍺2, presumably upon activation. This structural observation suggests that NINJ1 can form membrane disks, consistent with membrane fragmentation by recombinant NINJ1. Live-cell and super-resolution imaging uncover ring-like structures on the plasma membrane that are released into the culture supernatant. Released NINJ1 encircles a membrane inside, as shown by lipid staining. Therefore, NINJ1-mediated membrane disk formation is different from gasdermin-mediated pore formation, resulting in membrane loss and plasma membrane rupture. PubMed: 38614101DOI: 10.1016/j.cell.2024.03.008 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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