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. 2014 Oct 8;3:e04187. doi: 10.7554/eLife.04187

Figure 2. The crystal structure of PfRh5.

(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).

DOI: http://dx.doi.org/10.7554/eLife.04187.006

Figure 2—source data 1. Data collection and refinement statistics of Rh5 and Rh5_KI.
DOI: http://dx.doi.org/10.7554/eLife.04187.007
elife04187s001.docx (79.3KB, docx)
DOI: 10.7554/eLife.04187.007

Figure 2.

Figure 2—figure supplement 1. The secondary structure of PfRh5.

Figure 2—figure supplement 1.

Density for the N-terminal residues Asp127–Leu145, loop residues Glu258–Asn293, and C-terminal residues Met512–Gln526 was not observed. The helices and β-strands are colored red and green respectively. The vertical line at residue 119 and 319 indicates the position of a helical break.
DOI: http://dx.doi.org/10.7554/eLife.04187.008
Figure 2—figure supplement 2. Two free cysteine residues (Cys203 on α2a and Cys329 on α3b) within the crystal structure of PfRh5.

Figure 2—figure supplement 2.

The side chain of Cys329 is completely buried inside the three-dimensional fold of PfRh5 and the side chain of Cys203 is only partly exposed, consistent with the fact that no intermolecular disulfide bond was observed for the native and recombinant PfRh5.
DOI: http://dx.doi.org/10.7554/eLife.04187.009
Figure 2—figure supplement 3. Superimposition of the PfRh5 structure with N-terminal coiled-coil domain of SipB.

Figure 2—figure supplement 3.

The PfRh5 (green) coiled-coil helix bundle formed by helices α5, α6, and α7 has a very similar fold to the N-terminal coiled-coil domain of SipB (magenta).
DOI: http://dx.doi.org/10.7554/eLife.04187.010
Figure 2—figure supplement 4. A unique pocket on the surface of the PfRh5 molecule.

Figure 2—figure supplement 4.

(A) Location of the pocket on the surface formed by the β-hairpin, the triple-helical bundle, and the triple-helical coiled coil. (B) Close-up view of the pocket; key residues lining the pocket are labeled.
DOI: http://dx.doi.org/10.7554/eLife.04187.011