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Figure 1.
Fig. 1. Chemical structures of ribosome peptidyl transferase
substrates and analogs. (A) The tetrahedral carbon intermediate
produced during peptide bond formation; the tetrahedral carbon
is indicated by an arrow. (B) The transition state analog formed
by coupling the 3' OH of CCdA to the amino group of the O-methyl
tyrosine residue of puromycin via a phosphate group, CCdA-p-Puro
(a gift from Michael Yarus) (32). (C) An N-amino-acylated
mini-helix constructed to target the A-site. The oligonucleotide
sequence 5'-CCGGCGGGCUGGUUCAAACCGGCCCGCCGGA- CC-3' puromycin
should form 13 base pairs. The construct is based on a
mini-helix known to be a suitable substrate for amino-acylation
by Tyr-tRNA synthetase. The 3' OH of its terminal C is coupled
to the 5' OH of the N6-dimethyl A moiety of puromycin by a
phosphodiester bond.
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