A conserved secondary structural motif in 23S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation.
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.
Leviev
I G
IG
Institute of Molecular Biology, University of Copenhagen, Denmark.
Rodriguez-Fonseca
C
C
Phan
H
H
Garrett
R A
RA
Heilek
G
G
Noller
H F
HF
Mankin
A S
AS
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology*; D001483:Base Sequence; D017124:Conserved Sequence; D004352:Drug Resistance, Microbial / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects; D019617:Halobacterium salinarum / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D017354:Point Mutation; D014176:Protein Biosynthesis / Q000187:drug effects; D011741:Pyrimidine Nucleosides / Q000378:metabolism / Q000494:pharmacology; D012338:RNA, Ribosomal, 23S / Q000235:genetics* / Q000378:metabolism
D000900:Anti-Bacterial Agents; D011741:Pyrimidine Nucleosides; D012338:RNA, Ribosomal, 23S; C004413:amicetin