Figure 3 - full size

 

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.

The above figure is reprinted by permission from Cell Press: Cell (2000, 100, 551-560) copyright 2000.