Bfc. Clark et J. Nyborg, THE TERNARY COMPLEX OF EF-TU AND ITS ROLE IN PROTEIN-BIOSYNTHESIS, Current opinion in structural biology, 7(1), 1997, pp. 110-116
The past year has seen a breakthrough in our structural understanding
of how aminoacyl-tRNAs are selected and transported to the ribosomal A
-site in order to decode genetic information contained in messenger RN
A. All aminoacyl-tRNAs are recognized by the elongation factor EF-Tu i
n prokaryotes or EF-1 alpha in eukaryotes. The recent determination of
the structure of the ternary complex of aminoacyl-tRNA, EF-Tu and a G
TP analogue shows how the CCA end of all aminoacyl-tRNA structures can
be accommodated in a specific binding site on EF-Tu-GTP, and how part
of the T-helix can be recognized by EF-Tu in a non-sequence-specific
way. Furthermore, the structure of the ternary complex shows striking
structural similarity to the structure of another prokaryotic elongati
on factor, EF-G, the tRNA translocase, in its GDP or empty form. This
observation has led to the proposal of a general macromolecular mimicr
y of RNA and protein, which predicts elements of RNA-like structures w
ill occur in other translation factors, such as initiation factors and
release factors, that interact with similar sites on the ribosome.