Figure 5 - full size

 

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.

The above figure is reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2002, 21, 1987-1997) copyright 2002.