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Figure 9.
Figure 9. Conformational differences among concave TPR grooves
in TPR domains. To compare conformation and their binding
residues in TPR domains, the NrfG structure (orange) was
superimposed onto the corresponding CHIP (green) and HOP TPR1
(purple helices) with RMSDs of 2.31 Å and 2.07 Å,
respectively. The corresponding bound residues in the compared
TPR domains are represented in ball-and-stick fashion. These
comparisons show that the highly conserved Asn and Lys residues
in HOP and CHIP are mainly substituted by hydrophobic residues
(Ala, Leu) in NrfG. (A) The residues Glu81, Ala112, Tyr119, and
Thr145 of NrfG correspond to Asn 35, Asn 66, Lys 73, Lys96 of
CHIP [noted in the Fig. 5(A)], the residues of which are shown.
(B) The residues Ala77, Glu81, Ala112, Tyr119, Thr145, and
Leu149 of NrfG correspond to Lys8, Asn12, Asn43, Lys50, Lys73,
and Arg77 of HOP TPR1 [noted in the Fig. 5(B)], the residues of
which are shown.
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