(A) Ribbon representation of the PfRh5 structure. Color scheme is rainbow (N-terminus: blue; C-terminus: red) except for the β-hairpin that is colored magenta for clarity. The cysteine residues that form disulfide bridges (Cys345–Cys351 and Cys224–Cys317) are shown as spheres. Helices α4, α5, α6, and α7 assemble as a triplet-helical coiled-coil domain running the length of the long axis of the molecule, helices α1, α2a, and α3b assemble to form a short triplet-helical bundle and helices α2b and α3a assemble to form a short two-helix coiled coil. (B) Ribbon representation of the PfRh5 structure viewed after a 180o rotation relative to that in (A). The residues between Ser257 and Asp294 are disordered. (C) Ribbon representation of the PfRh5 structure viewed from the side with the C-terminus on the left. The disulfide bridges are indicated with arrows. (D) Ribbon representation of the PfRh5 structure viewed after a 180o-rotation relative to that in (C).