Biology Reference
In-Depth Information
Figure 7.5 The structure of ThkA/TrrA complex from (A) side view and (B) top view. The
complex forms 2:2 dimer with protomers A and B.
region corresponding to the FG loop in FixL (
Fig. 7.6
), which suggests that a
conformational change in the FG loop may induce directly conformational
changes in the kinase catalytic domain of FixL through reconstructions of
the interdomain interactions.
ThkA forms a homodimer, in which the four-helix bundle formed by
two DHp domains is responsible for dimerization of two protomers
(
Yamada et al., 2009
). His547 that is phosphorylated in ThkA is located
at the C-terminal region of the
a
6 helix in the DHp domain. In the
