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Figure 5.
Figure 5. a, Contacts between the AAD and the upper surface of
the ANK core. The AAD is shown as a coil with side chains
attached. The molecular surface of the ANK is colored white, and
the surface associated with atoms within van der Waals contact
of the AAD is colored red. b, Residues within the first ANK
repeat of Swi6 (left) generate an extensive hydrophobic surface
(red) that is partially occluded through interactions with the
AAD (shown as blue coil). Mapping sequence substitutions in Swi4
(right) and Mbp1 (not shown) onto the Swi6 backbone structure
shows that this surface is conserved and suggests that a similar
AAD−like structure is likely to be present in these and the
other Swi6−related proteins. The surface associated with the
conserved Swi6 Trp 344 is colored blue. Parts (a) and (b)
produced using GRASP^61. c, Homology within the region
immediately N−terminal to the ANK core of Swi6/Cdc10−related
proteins. The homologous cluster of nonpolar residues and the
N−terminal segment of the first ANK repeat are boxed. Figs 4
and 5c produced using ALSCRIPT^62.
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