|
Figure 3.
Fig. 3. Comparison of RNA binding motifs in the OB folds
of EMAP II and AspRSSC (23) structures. The orientations and
residues are the same as described for Fig. 2A. The nomenclature
of secondary structure elements follows the same convention as
used in Figs. 1C and 2B. A, anticodon binding motif of AspRSSC.
The 5 residues are shown to interact specifically with the three
anticodon bases of Asp-tRNA by hydrogen bonds. Loop L5 is
oriented so that it forms a valley to generate the binding
pocket for the anticodon bases of Asp-tRNA. N represents the
location of Ser-105 and C the location of Ser-198. B, RNA
binding motif of EMAP II. The probable candidate residues, which
may interact with tRNAs nonspecifically, are inferred from a
comparison of the conserved residues in the EMAP II-like domains
(4) with those involved in anticodon base interactions in the
AspRSSC structure (23). The 5 hydrophilic residues are
positioned in the smooth surface formed by loop L4, the strands
 5i and 6i headed to
the C terminus, whereas the residues of AspRSSC form a valley
for the binding pocket of anticodon bases. N represents the
location of Arg-8 and C the location of Pro-87.
|
