ABC toxins are bacterially secreted pore-forming toxins of ~2 MDa in size, and are strongly implicated in insect and human pathogenicity. These multi-chain protein complexes have a tripartite architecture in which the A subunit specifically recognises the host cell membrane in the pre-pore conformation, and subsequently perforates the membrane to enable translocation of a cytotoxin (subunit C) through a pore domain. This mechanism of pore formation and toxin translocation is accompanied by substantial structural domain rearrangements and prior to now, it has remained unclear whether these mechanisms are shared across the ABC toxin family or with any other pore-forming toxins. Here we present cryo-EM structures of the Yersinia entomophaga toxin complex, YenTc, which is representative of a novel ABC toxin subtype. Our cryo-EM data was solely collected on a ThermoFisher Tecnai F30 TEM, equipped with a Gatan K2 direct electron detector, demonstrating that near atomic resolution structures can be obtained on a low throughput microscope and holder, without automated screening and data collection. We achieved map resolutions ranging from beyond 4 Å in the rigid pore regions to ~10 Å at the flexible periphery. We determined structures of samples prepared with various solubilisation methods, representing different conformational states of the holotoxin. Subsequent to initial refinements of the full holotoxin, we improved the resolution of several subdomains using focused 3D refinement. Taken together, our models provide a comprehensive, 4D picture of YenTc with insights into the molecular drivers of physiologically relevant conformational changes as well as mechanisms of host recognition of two exposed and enzymatically active chitinases. In providing a structural framework for understanding the mechanisms of target-specific peptide delivery by YenTc, we hypothesise that this work will also inform strategies for engineering YenTc (and ABC toxins in general) to be used as modifiable toxin delivery systems in therapeutic applications.