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Figure 3.
Figure 3. Structure of Δ50Tom20 in Complex with a
Presequence Peptide, pALDH(12–22)(A) Sequence alignment of
Δ50Tom20 and corresponding regions of Tom20 from other
organisms (human, Caenorhabditis elegans, Neurospora crassa, and
yeast Saccharomyces cerevisiae). The two acidic regions and the
Q-rich region are shaded in red and yellow, respectively. The
TPR motif is shown as a blue box with its consensus amino acids.
α helices and flexible regions are drawn as cylinders and
broken lines, respectively. The hydrophobic residues
constituting the hydrophobic patch in the presequence binding
groove are indicated with yellow triangles, and the hydrophilic
residues in the periphery of the groove are colored in orange
(Gln) and red (Glu) circles.(B) Overlay of the 20 final
structures. The residues used for superimposing the different
structures are colored in blue (Tom20) and red (presequence
peptide), and the other residues are in gray (Tom20) and orange
(presequence).(C) Ribbon model of Δ50Tom20 indicating the
{^1H}-^15N heteronuclear NOE values (red to white; −0.9  vert,
similar +0.9) measured in the absence of the presequence.
Smaller NOE values imply faster motions.
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