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Figure 3.
Figure 3 Conserved residues and electrostatic potential on the
surface of UvrB. For a better view into the ATP binding site,
domain 3 has been rotated by 120° away from the remainder of
UvrB to show the interface between domains 1a and 3. The ATP
molecule has been duplicated in the figure, shown in its
orientation with respect to domains 1a and 3. Residues 96 -98
and 109 -113 were omitted from the surface calculation and are
shown as a cyan backbone worm for a better view into the cleft
between domains 1a and 1b. (A) Side chains on the surface of
UvrB that are conserved throughout 16 UvrB sequences are colored
according to their location in helicase motifs I-VI. Magenta,
motifs I and IV; green, motifs II and V; blue, motifs III and
VI; yellow, conserved residues not belonging to any helicase
motif. (B) Electrostatic potential calculated separately for
domain 3 and for the remainder of the molecule including the
bound ATP, at an ionic strength of 0.1 M contoured at  10
k[B]T (k[B] is the Boltzmann constant and T the absolute
temperature). Blue, positively charged; red, negatively charged.
Figures 3 and 5 were made using GRASP (Nicholls et al., 1991).
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