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Figure 4.
The conformational changes of Tom71 generated by Hsp70
binding.a, the N-terminal domain of Tom71 is superimposed with
that in the Tom71-Hsp70 complex and they are shown by a ribbon
drawing. The Tom71 N-terminal domain is in light blue. The Tom71
N-terminal domain within the Tom71-Hsp70 complex is in silver.
The bound Hsp70 C-terminal peptide is in red. Helices A5, A6,
and A7 are labeled in blue. Some residues of Tom71 involved in
generating the conformational changes are labeled in black.
Residues Lys^196, Arg^200, and Leu^199 of Tom71 involved in
binding Hsp70 are labeled. The residues forming hydrophobic
cluster to associate A5, A6, and A7 are labeled. Glu^206 and
Arg^238 linking A5 and A7 by forming a salt bridge are also
labeled. b, Cα trace drawings of yeast Tom71 structure and the
Tom71-Hsp70 complex structure. The N-terminal domain of Tom71 is
superimposed with that in the Tom71-Hsp70 complex structure. The
molecules in this figure are in a similar orientation as in a.
The uncomplexed Tom71 structure is in purple. In the Tom71-Hsp70
C terminus complex, Tom71 is in green, and the Hsp70 C terminus
is in red. The N- and C-terminal domains of Tom71 are labeled.
Helix A7 acting as the hinge to connect the N-and C-terminal
domains of Tom71 is labeled.
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