page_title: 23S ribosomal RNA
hierarchical_section_title: 23S ribosomal RNA
caption_attribution_description: Secondary structure image for PK-G12rRNA non coding RNA (RF01118). Nucleotide colouring indicates sequence conservation between the members of this family.
context_page_description: The 23S rRNA is a 2904 nt long component of the large subunit of the bacterial/archean ribosome. The ribosomal peptidyl transferase activity resides in domain V of this rRNA, and this domain is the most common binding site for antibiotics that inhibit translation. A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Linezolid and quinupristin-dalfopristin also bind to the 23S rRNA, and cross-resistance has been demonstrated between these antibiotics. Compared to 16S rRNA genes, 23S rRNA genes typically have higher sequence variations including insertions and/or deletions.
  The eukaryotic homolog of the 23S rRNA is the 28S ribosomal RNA, with a region filled by the 5.8S ribosomal RNA.
context_section_description: The 23S rRNA is a 2904 nt long (in E. coli) component of the large subunit (50S) of the bacterial/archean ribosome. The ribosomal peptidyl transferase activity resides in domain V of this rRNA, and this domain is the most common binding site for antibiotics that inhibit translation. A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Linezolid and  quinupristin-dalfopristin also bind to the 23S rRNA, and cross-resistance has been demonstrated between these antibiotics. Compared to 16S rRNA genes, 23S rRNA genes typically have higher sequence variations including insertions and/or deletions.
  The eukaryotic homolog of the 23S rRNA is the 28S ribosomal RNA, with a region filled by the 5.8S ribosomal RNA.
caption: Predicted secondary structure and sequence conservation of PK-G12rRNA
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