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Figure 4.
Figure 4. Structure of the Plasmodium falciparum Profilin
Bound to an Octaproline Peptide
(A) Overview of the
structure with the peptide. The N- and C-terminal helices (α1
and α4, respectively) are labeled.
(B) Structure of the
polyproline-binding site. The side chains of the 4 aromatic
residues forming the binding site are shown. The C-terminal
α-helix (α4) does not participate in binding interactions as
in mammalian and yeast profilins; instead, the N terminus turns
back toward the peptide (in orange), allowing the
Plasmodium-specific Tyr5 to engage in an intimate interaction
with the peptide (Figure S3). The two direct hydrogen bonds
between the peptide and side chains of Tyr5 and Trp7 are shown
as dashed lines. The N and C termini of the octaproline peptide
are indicated. The electron density shown is the final refined
2F[o]–F[c] map contoured at 1 σ.
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