Structural highlights
Function
GSDM_RUNZN Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Cleavage of this precursor by its dedicated, neighboring protease (G563DRAFT_02009) releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and triggering cell death (PubMed:35025633). Expression of bGSDM and its protease is highly toxic in E.coli (PubMed:35025633). Cells expressing the gene pair stop dividing and lose membrane integrity (PubMed:35025633). Both proteins are required to kill E.coli (PubMed:35025633).[UniProtKB:A0A0S2DNG5][1] Pore-forming protein that causes membrane permeabilization via a pyroptosis-like activity (PubMed:35025633). Makes ring-like pores with walls about 50 Angstroms thick and an interior pore diameter of 200-300 Angstroms, when integrated in liposomes (PubMed:35025633, PubMed:38509367).[2] [3]
References
- ↑ Johnson AG, Wein T, Mayer ML, Duncan-Lowey B, Yirmiya E, Oppenheimer-Shaanan Y, Amitai G, Sorek R, Kranzusch PJ. Bacterial gasdermins reveal an ancient mechanism of cell death. Science. 2022 Jan 14;375(6577):221-225. doi: 10.1126/science.abj8432. Epub 2022, Jan 13. PMID:35025633 doi:https://dx.doi.org/10.1126/science.abj8432
- ↑ Johnson AG, Wein T, Mayer ML, Duncan-Lowey B, Yirmiya E, Oppenheimer-Shaanan Y, Amitai G, Sorek R, Kranzusch PJ. Bacterial gasdermins reveal an ancient mechanism of cell death. Science. 2022 Jan 14;375(6577):221-225. doi: 10.1126/science.abj8432. Epub 2022, Jan 13. PMID:35025633 doi:https://dx.doi.org/10.1126/science.abj8432
- ↑ Johnson AG, Mayer ML, Schaefer SL, McNamara-Bordewick NK, Hummer G, Kranzusch PJ. Structure and assembly of a bacterial gasdermin pore. Nature. 2024 Apr;628(8008):657-663. PMID:38509367 doi:10.1038/s41586-024-07216-3