Wiley - Devlin's Textbook of Biochemistry

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FIGURE 17.6
Interaction of a tRNA with its cognate aminoacyl-tRNA synthetase.
Figure shows sugar-phosphate backbone of E. coli glutaminyl tRNA in red and the peptide backbone of the glutamine tRNA^Gln synthetase in black. Note the strong interactions of the synthetase with both the partially unwound acceptor stem the and anticodon loop of the tRNA, and placement of ATP, shown in green, within a few angstroms of the 3' end of tRNA. Space-filling models of the enzyme and tRNA would show both molecules to be solid objects with several sites of direct contact.
Adapted from J. Perona, M Rould, and T. Steitz, Biochemistry 32:8758, 1993.

FIGURE 17.23
Model of proteasome.
A 20S central segment is made up of four stacked heptameric rings of two types. The core is hollow and includes 12-15 different polypeptides; several proteases with different specificities are localized within the rings. V-shaped segments at each end cap the cylinder and are responsible for ATP-dependent substrate recognition, unfolding, and translocation into the proteolytic core. Upper cap structure is also in contact with the central segment but it is shown displaced from it in order to illustrate the hollow core of the cylinder.
Adapted from D. Rubin and D. Finley, Curr. Biol. 5:854, 1995; and J.-M. Peters, Trends Biochem. Sci. 19:377, 1994.