Figure 3.
Figure 3 Recognition of the puromycin by E. coli
L/F-transferase. (A) Chemical structure of puromycin (left) and
that of the 3'-ends of Leu-tRNA^Leu and Phe-tRNA^Phe (middle and
right, respectively). The amino-acid moiety and the base moiety
are colored pink and blue, respectively. (B) |Fo-Fc| omit map of
puromycin (contour level 3.0 ).
(C) Recognition of the p-methoxybenzyl group and the puromycin
base by the hydrophobic pocket, as shown by a surface model. (D)
Ribbon model of (C). The hydrophobic amino acid involved in the
recognition of the p-methoxybenzyl group and the base moiety of
puromycin are colored green and blue, respectively. (E) The
C-shaped edge of the hydrophobic pocket is composed of
continuous amino-acid residues (Gly155-Glu156-Ser157-Met158;
colored yellow and highlighted). The -,
-
and -carbons
of puromycin are also shown.
).
(C) Recognition of the p-methoxybenzyl group and the puromycin
base by the hydrophobic pocket, as shown by a surface model. (D)
Ribbon model of (C). The hydrophobic amino acid involved in the
recognition of the p-methoxybenzyl group and the base moiety of
puromycin are colored green and blue, respectively. (E) The
C-shaped edge of the hydrophobic pocket is composed of
continuous amino-acid residues (Gly155-Glu156-Ser157-Met158;
colored yellow and highlighted). The 
-,
-
and 
-carbons
of puromycin are also shown.