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. 2009 Jul 6;284(35):23852–23859. doi: 10.1074/jbc.M109.023986

FIGURE 3.

FIGURE 3.

The complex structures of Tom71 and the Hsp70/Hsp90 C-terminal EEVD motif. a, the surface potential drawing of Tom71 complexed with Hsp70 C-terminal peptide PTVEEVD. Tom71 is shown in surface potential drawing generated by Pymol and Apbs. Blue and red denote positively and negatively electrostatic potentials, respectively. The bound Hsp70 peptide is shown in a rod model. In the rod model, carbon atoms are shown in green, oxygen atoms are shown in red, and nitrogen atoms are shown in blue. To indicate the enlargement of the preprotein-binding pocket of Tom71 after Hsp70 binding, the distance (32 Å) between Pro234 and Phe496 of Tom71 is shown. b, the surface potential drawing of Tom71 N-terminal domain interacting with the Hsp70 C-terminal peptide PTVEEVD in a rod model. The residues of Tom71 involved in binding Hsp70 are labeled in green, and the residues of Hsp70 peptide PTVEEVD are labeled in black. c, ribbon drawing of Tom71 N-terminal domain complexed with Hsp70 C terminus in stereo mode. Tom71 is in a silver ribbon drawing, and the Hsp70 C-terminal peptide is in a solid rod model. The residues of Tom71 involved in binding Hsp70 are drawn in dotted rod model and labeled in blue. The residues of Hsp70 peptide are labeled in black. d, the surface potential drawing of Tom71 N-terminal domain interacting with Hsp90 C-terminal peptide MEEVD in a rod model. The residues of Tom71 involved in binding Hsp90 are labeled in green, and the residues of Hsp90 peptide MEEVD are labeled in black.