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Figure 5.
Figure 5 GRASP (Nicholls et al., 1991) representations of the
protein−RNA complex showing the symmetric role of the CAT
monomers and the cavity on each side of the dimer receiving the
bulged-out base in the RNA internal loop 1 (left side views) and
loop 2 (right side views). In each case, the left and right side
views showing the protein surface and the RNA backbone are
rotated by 180°
with respect to each other. (A) The protein monomers are
coloured in red and blue as in Figure 3. Amino acid residues are
labelled in black. The bulged-out bases are labelled in white.
(B) The electrostatic surface potential as calculated for the
free CAT dimer using GRASP. The amino acids lying in the minor
groove of the RNA helix are essentially neutral. They are
surrounded by two spines of basic residues, interacting with the
phosphodiester backbone. (C) Conserved amino acids and
nucleotides coloured as a function of their level of
conservation among the LicT/SacY family. Strictly conserved
amino acids within the AT family are coloured in dark blue,
conserved residues in blue and others in green. Similarly, the
nucleotides are coloured in red, orange, yellow and green as
their level of conservation within the RAT sequences decreases.
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