Peptidyl transferase center of ribosome (PTC)

The peptidyl transferase center of the ribosome (PTC) is the highly conserved catalytic core of the large ribosomal subunit, composed primarily of 23S (prokaryote) or 28S (eukaryote) ribosomal RNA, and is responsible for catalyzing peptide bond formation between amino acids during translation, as well as hydrolyzing peptidyl-tRNA to release the completed polypeptide at translation termination[1][2][3][5]. Unlike most enzymes, the PTC is a ribozyme, with catalytic activity provided by RNA rather than protein. It achieves catalysis mainly through substrate positioning and electrostatic stabilization, rather than chemical catalysis by amino acid side chains[1][2][5]. The PTC represents one of the most evolutionary ancient features of biology and is the target of many clinically important antibiotics, which bind to the PTC to inhibit protein synthesis—often with species- or domain-specific differences in binding and resistance[2][3][4]. Resistance to PTC-targeting drugs often arises through mutations or methylation of specific rRNA nucleotides, providing clinically relevant biomarkers for antibiotic selection and monitoring[2][3]. The PTC is essential for life, and its function and structure have remained highly conserved throughout evolution[1][5]. Caveat: The PTC is not a protein or a classic "receptor"—it is an RNA-based catalytic site. Its function as a drug target is of paramount importance in infectious diseases, particularly in the action and resistance to antibiotics, but it is not a "disease gene" in the conventional sense since its essentiality is universal across all domains of life.

Other names

Peptidyl transferase centerRibosomal peptidyl transferase centerRibosome PTC

Inhibition of peptide bond formation (by antibiotics binding to the PTC); Inhibition of peptidyl-tRNA hydrolysis (antibiotics and stalling peptides); Allosteric modulation via nascent peptide-induced stalling