23S ribosomal RNA–ribosomal protein uL11–elongation factor G translocation site (SRL–uL11–EF-G site)

The SRL–uL11–EF-G site in prokaryotic ribosomes is the functional center for GTP hydrolysis and translocation during protein synthesis. 23S rRNA forms the core of the large subunit and contains the sarcin-ricin loop, which interacts with the GTPase domain of EF-G, a translation factor responsible for catalyzing mRNA and tRNA movement across the ribosome after each peptide bond is formed. Ribosomal protein uL11, together with adjacent rRNA sequences, helps organize the L11 stalk, facilitating interactions with EF-G and other translational GTPases. The precise arrangement and dynamic interactions of these components are essential for the rapid and accurate translocation of substrates needed for protein synthesis, and they represent major targets for antibiotics such as fusidic acid, which inhibits translocation by preventing EF-G dissociation after GTP hydrolysis.

Other names

Sarcin-ricin loop–L11 stalk–EF-G complexGTPase activation center (in the ribosome)

Antibiotic binding blocks conformational changes essential for EF-G-mediated translocation and/or GTP hydrolysis, stalling protein synthesis