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A conserved secondary structural motif in 23S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation.
Author(s) -
Leviev I.G.,
RodriguezFonseca C.,
Phan H.,
Garrett R.A.,
Heilek G.,
Noller H.F.,
Mankin A.S.
Publication year - 1994
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1994.tb06432.x
Subject(s) - library science , biology , computer science
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.