The adaptor protein PTEX150 and disordered regions in Plasmodium proteome. (A) Schematic organization of PTEX150, including SS, signal sequence. Only ~18% of the total protein, corresponding to the core and spike domains, are resolved in the structure. (B) The PTEX150 protomer structure in transparent surface representation. The core of one PTEX150 protomer can be divided into an outer and inner ‘wall’ separated by a bridge and sits on top of the vestibular domain of the EXP2 protomer (colored as in Figure 3). The hydrophilic inner wall contributes to the lining of the central pore. A model helix (P) indicates the axis of the central pore along the protein-conducting path (transparent grey cylinder). (C) Heptameric arrangement of PTEX150. (D) Schematic showing the overall contribution of the disordered/flexible protein regions in PTEX. Egea PF. Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites. Microorganisms. 2020 8(6):865. PMID: 32521667