The study investigates the structure and assembly of bacterial gasdermin (bGSDM) pores, which are formed by bGSDMs in response to pathogen infection to induce pyroptosis in host cells. The researchers engineered a panel of bGSDMs for site-specific proteolytic activation and found that these proteins form pores of varying sizes, ranging from smaller mammalian-like assemblies to larger pores containing over 50 protomers. They determined a 3.3 Å cryo-EM structure of a *Vitiosangium* bGSDM in an active slinky-like oligomeric conformation and analyzed bGSDM pores in a native lipid environment to create an atomic-level model of a full 52-mer bGSDM pore. The results support a stepwise model of GSDM pore assembly and suggest that a covalently bound palmitoyl can leave a hydrophobic sheath and insert into the membrane before forming the membrane-spanning β-strand regions. The study reveals the diversity of GSDM pores in nature and explains the function of an ancient post-translational modification in enabling programmed host cell death.The study investigates the structure and assembly of bacterial gasdermin (bGSDM) pores, which are formed by bGSDMs in response to pathogen infection to induce pyroptosis in host cells. The researchers engineered a panel of bGSDMs for site-specific proteolytic activation and found that these proteins form pores of varying sizes, ranging from smaller mammalian-like assemblies to larger pores containing over 50 protomers. They determined a 3.3 Å cryo-EM structure of a *Vitiosangium* bGSDM in an active slinky-like oligomeric conformation and analyzed bGSDM pores in a native lipid environment to create an atomic-level model of a full 52-mer bGSDM pore. The results support a stepwise model of GSDM pore assembly and suggest that a covalently bound palmitoyl can leave a hydrophobic sheath and insert into the membrane before forming the membrane-spanning β-strand regions. The study reveals the diversity of GSDM pores in nature and explains the function of an ancient post-translational modification in enabling programmed host cell death.