Figure 1.
Figure 1. (A) Alignment of the ribosomal protein L27
sequences from T. thermophilus HB8, D. radiodurans, and E. coli.
The multiple alignment was achieved with CLUSTAL X (Thompson et
al. 1997). The secondary structural elements, determined on the
basis of the X-ray structure of T. thermophilus protein L27, are
indicated with arrows for -strands and a
coil for a 3[10] helix at the top of the alignment. The
identical amino acid residues are shown in white letters
highlighted in red, whereas the similar residues are shown in
red letters. (B) Stereo structure of the T. thermophilus protein
L27. The stereo views were prepared by the programs MOLSCRIPT
(Kraulis et al. 1991) and RASTER3D (Merritt and Bacon 1997). (C)
Electrostatic potential surface of the T. thermophilus ribosomal
protein L27. The molecular surface presentation was generated by
GRASP (Nicholls et al. 1991).
The above figure is reprinted
by permission from the Protein Society:
Protein Sci
(2004,
13,
2806-2810)
copyright 2004.
-strands and a
coil for a 3[10] helix at the top of the alignment. The
identical amino acid residues are shown in white letters
highlighted in red, whereas the similar residues are shown in
red letters. (B) Stereo structure of the T. thermophilus protein
L27. The stereo views were prepared by the programs MOLSCRIPT
(Kraulis et al. 1991) and RASTER3D (Merritt and Bacon 1997). (C)
Electrostatic potential surface of the T. thermophilus ribosomal
protein L27. The molecular surface presentation was generated by
GRASP (Nicholls et al. 1991).