|
Figure 3.
The structure of the Y72A mutant reveals cleaved AP DNA
(a) and ordered water molecules (b) adjacent to the cleaved AP
site (3  light
blue and 4 dark
blue contoured omit maps). Panels a and b are drawn in
stereoview. (c) The structures of wild-type (left) and Y72A
mutant (right) Endo IV bound to AP DNA product are virtually
superimposable. Removal of the Tyr72 side chain allows increased
solvation of the active site.
|
