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. 1994 Apr 1;13(7):1682–1686. doi: 10.1002/j.1460-2075.1994.tb06432.x

A conserved secondary structural motif in 23S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation.

I G Leviev 1, C Rodriguez-Fonseca 1, H Phan 1, R A Garrett 1, G Heilek 1, H F Noller 1, A S Mankin 1
PMCID: PMC394999  PMID: 8157007

Abstract

The binding site and probable site of action have been determined for the universal antibiotic amicetin which inhibits peptide bond formation. Evidence from in vivo mutants, site-directed mutations and chemical footprinting all implicate a highly conserved motif in the secondary structure of the 23S-like rRNA close to the central circle of domain V. We infer that this motif lies at, or close to, the catalytic site in the peptidyl transfer centre. The binding site of amicetin is the first of a group of functionally related hexose-cytosine inhibitors to be localized on the ribosome.

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