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Figure 3.
Figure 3 (A) General view of the dimeric aspartyl-tRNA
synthetase from E.coli complexed with yeast tRNA^Asp and
aspartyl-adenylate. The tRNA^Asp molecules, colored in red and
yellow, are bound to one protein subunit shown in brown and
white, respectively. (B) AspRS surface buried by the tRNA in
monomer 1 (left) and monomer 2 (right) calculated and displayed
using GRASP (Nicholls and Honig, 1991). The surface is colored
according to a distance array between the two molecular
surfaces: distances <2.5 Å between the tRNA and the enzyme are
drawn in green, and distances between 2.5 and 3.5 Å are in
yellow. The interaction surfaces are highly similar for the
protein N-terminal domain in both monomers but vary through the
rest of the complex. (C) Ribbon representation of one AspRS
subunit in gray (monomer 1) of the heterologous complex with the
bound yeast tRNA^Asp in yellow. The E.coli tRNA^Asp as seen in
the cognate complex is drawn in blue after superposition of the
enzymes on their active sites. (D) Relative position of the two
tRNAs of the heterologous complex. Superposition was optimized
on the two subunit active sites. The tRNA^Asp from monomer 1 is
drawn in yellow, the tRNA from monomer 2 in red. (E) Comparison
of the tRNA molecule from monomer 2 of the heterologous complex
(red) and the free (uncomplexed) yeast tRNA^Asp (green) (Moras
et al., 1980). Figures 3, Figures 4, 5 were generated using the
Program SETOR (Evans, 1998).
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