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Figure 3.
Figure 3. The τ60/Δτ91 Interface
(A) Stereo diagram
of the interactions between τ60 and Δτ91. The view
corresponds to Figure 1A. Hydrogen bonds are indicated as dashed
lines. Blades and strands involved in the interactions are
indicated for both proteins.
(B) Summary of the
interactions between τ60 and Δτ91. Strands, labeled from A to
D, are represented by arrows. Hydrophobic, polar, basic, and
acidic residues are in green, orange, blue, and red,
respectively. Polar interactions involving main chain atoms are
indicated as dashed gray lines, polar interactions between side
chain atoms as gray lines, and hydrophobic interactions as green
lines. The blades are labeled for both proteins.
(C)
Conservation and electrostatic surface potentials of the τ60
and Δτ91 contact surfaces. The left and right panels show
charge distribution (top) and sequence conservation (bottom) of
the τ60 and Δτ91 contact surfaces, respectively. Sequence
conservation above 70% is depicted in green based on a sequence
alignment of different fungal orthologs (Figures S1 and S2).
Dashed yellow lines indicate interacting regions. Regions of
negative and positive surface potential are depicted in red and
blue, respectively. Figures 3C and 4C were generated with the
program GRASP (Nicholls et al., 1993).
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