50S ribosomal protein L27 (bL27) (bL27)

50S ribosomal protein L27 (bL27) is an essential component of the large subunit of the bacterial ribosome, located at the peptidyl transferase center (PTC) (UniProt: P0A7L8). The N-terminal tail of bL27 reaches into the catalytic heart of the ribosome, where it facilitates the orientation of tRNA molecules and stabilizes the transition state during peptide bond formation (PubMed: 15131269). Due to its central location, bL27 is a key structural element of the binding site for various clinically important antibiotics, including macrolides, lincosamides, and pleuromutilins (PubMed: 25108352). These drugs typically bind to the 23S rRNA in the PTC or the nascent peptide exit tunnel, and the presence of bL27 is crucial for the overall architecture of these drug-binding pockets. Mutations in bL27 or its absence can significantly reduce the rate of protein synthesis and alter the susceptibility of bacteria to these antimicrobial agents. As a highly conserved protein in bacteria, it is a significant target for understanding the mechanisms of translation and the development of new antibiotics to combat multi-drug resistant pathogens (PubMed: 17113138).

Other names

Ribosomal protein L27rpmA50S ribosomal protein L27

Inhibition of bacterial protein synthesis by interfering with the peptidyl transferase center (PTC) or the nascent peptide exit tunnel (NPET).