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The **23S ribosomal RNA** is a large non-coding RNA molecule (~2900 nucleotides in *E. coli*) that forms an essential part of the **50S large subunit** of prokaryotic and archaeal ribosomes. It constitutes the core catalytic component known as the **peptidyl transferase center**, which is responsible for catalyzing peptide bond formation during protein synthesis. The structure consists of six secondary domains, providing both structural integrity and functional sites critical for translation. Many clinically important antibiotics—including macrolides, lincosamides, oxazolidinones, and chloramphenicol—target this molecule by binding to its active site(s), thereby inhibiting bacterial protein synthesis. Mutations or chemical modifications within key regions confer antibiotic resistance and may impact cell viability or growth phenotypes. The eukaryotic homolog is called **28S rRNA**.[1][2][3][5]
Inhibition of peptide bond formation by binding to the peptidyl transferase center, blocking protein synthesis[2][6]; Prevention of tRNA binding or translocation within the ribosome[2]
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