Correlations, Fourth Edition
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Interaction of a tRNA with its cognate aminoacyl-tRNA
Figure shows sugar-phosphate backbone of E. coli
glutaminyl tRNA in red and the peptide backbone of the
glutamine tRNAGln 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.
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.
Textbook of Biochemistry With Clinical Correlations, Fourth Edition
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