Bacterial 50S ribosomal subunit L11-binding site (50S L11-binding site)

The Bacterial 50S ribosomal subunit L11-binding site is a critical functional region within the large ribosomal subunit, primarily composed of a complex between the 23S ribosomal RNA and the L11 ribosomal protein (Harms et al., 2008, Molecular Cell). This site forms part of the GTPase-associated center (GAC), which is essential for recruiting and activating translational GTPases such as Elongation Factor G (EF-G) and Elongation Factor Tu (EF-Tu) (Voorhees et al., 2010, Science). By facilitating the interaction between these factors and the ribosome, the site plays a pivotal role in the translocation of mRNA and tRNAs during protein synthesis. It is a well-characterized target for thiopeptide antibiotics, such as thiostrepton and micrococcin, which bind at the interface of the rRNA and L11 protein to sterically hinder factor binding (Bagley et al., 2005, Chemical Reviews). Because the structural features of this site are highly conserved across bacterial species but differ significantly from the eukaryotic 60S subunit, it represents a high-affinity target for selective antimicrobial agents. Targeting this secondary site provides an alternative mechanism to traditional antibiotics that focus on the peptidyl transferase center or the nascent peptide exit tunnel.

Other names

Bacterial 50S ribosomal subunit secondary RNA/protein siteGTPase-associated centerGAC23S rRNA-L11 complexThiopeptide binding siteL11-binding domain

Inhibition of translation elongation by sterically blocking the binding of elongation factors EF-G and EF-Tu to the GTPase-associated center.