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Figure 5.
Figure 5. Structure-based optimization of the G design. The
DNase is colored in teal and the immunity protein in gray.
Residues participating in the interaction that have been changed
or were allowed to vary are shown in space-fill representation,
in green and yellow, respectively. (a) In the G design crystal
structure the T516 hydroxyl group makes a hydrogen bond to the
backbone carbonyl of I54, but the methyl group of the threonine
is sub-optimally packed. (b) In the wild-type interface N516
forms a water-mediated (magenta) hydrogen bond to the backbone
carbonyl of I54. Following sequence optimization surrounding
T516 using the G design structure, the two sequences with the
lowest predicted binding energies contained the L19V/I68F(c) and
I68W mutations (d) (named G_68F and G_68W, respectively).
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