Detailed views of the PTEX protein-conducting channel and symmetry mismatch in the engaged state. CryoEM densities and atomic models of cargo and pore loops from the near-atomic resolution structures of Clp/HSP100 ATPases YME1 (a), PTEX HSP101 (b), and HSP104 (c). Tyrosine sidechain densities are clearly visible intercalating with the cargo densities. The modeled engaged state PTEX cargo has a calculated RMSD of 1.09Å and 1.25Å to the published YME1 and HSP104 cargo models, respectively. Pore loops are labeled by NBD and protomer (e. g., D2PL,P1: NBD2 Pore Loop, Protomer 1). d, Side view of the bisected engaged state PTEX cryoEM map. The protein-conducting channel, calculated using HOLE, is shown superimposed over the bisected map in translucent white with a navy outline. The HSP101 NBD2 pore loop densities are colored by HSP101 protomer, and the cargo density is colored pink. e-j, The transition from the assymetric HSP101 spiral to the C7 pseudosymmetric PTEX150(668–823)-EXP2 heptamer is depicted using a series of cross sections taken perpendicular to the central axis of the translocon, spanning the area of symmetry mismatch. The section of the translocon corresponding to each cross-sectional image is indicated with a brackets in (d). Ho CM, Beck JR, Lai M, Cui Y, Goldberg DE, Egea PF, Zhou ZH. Malaria parasite translocon structure and mechanism of effector export. Nature. 2018 561(7721):70-75.