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The **23S ribosomal RNA in the 50S ribosomal subunit** is a large, highly conserved ribonucleic acid molecule (~2,900 nucleotides in E. coli) that forms the core of the bacterial large ribosomal subunit (50S)[3]. It is the principal component of the ribosomal *peptidyl transferase center* (PTC), which catalyzes peptide bond formation during translation[2][3]. The 23S rRNA is arranged in six structural domains, interacts with both ribosomal proteins and tRNAs, and is critical for ribosome assembly and function[1][4]. Multiple classes of clinically important antibiotics exert their effects by binding to specific sites on the 23S rRNA, inhibiting protein synthesis; mutations or chemical modifications (e.g., methylation at specific nucleotides like U2552) can confer resistance and are important clinical biomarkers[3][5]. While not a receptor or enzyme in the conventional drug-target sense, the 23S rRNA is a validated and essential target for numerous antibiotics and is central to the biology of bacterial infection[3].
Inhibition of peptidyl transferase activity; Blockage of the peptide exit tunnel; Disruption of tRNA positioning at the A or P site; Allosteric modulation of ribosome conformation
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