Elongation factor G (EF-G) – ribosome complex (EF-G – ribosome complex)

The Elongation factor G (EF-G) – ribosome complex is a fundamental component of the bacterial protein synthesis machinery, responsible for the translocation step of translation (UniProt, 2024). Elongation factor G, a translational GTPase encoded by the fusA gene, binds to the ribosome and utilizes the energy from GTP hydrolysis to move the mRNA and tRNAs through the ribosomal subunits, a process essential for the continuous elongation of the polypeptide chain (PubMed, 2023). This complex serves as a primary target for several classes of antibiotics, most notably the steroid-like antibiotic fusidic acid, which prevents the release of EF-G from the ribosome after GTP hydrolysis (StatPearls, 2024). By stalling the ribosome in a post-translocational state, these drugs effectively inhibit bacterial growth and protein production. Mutations in the fusA gene are a common mechanism of clinical resistance, often reducing the affinity of the drug for the complex (NIH, 2022). Additionally, the complex plays a role in ribosome recycling, where EF-G works alongside ribosome recycling factor (RRF) to disassemble the post-termination complex. Given its essentiality in bacteria and structural differences from eukaryotic counterparts, it remains a key focus for antimicrobial drug discovery and structural biology research.

Other names

EF-GTranslocaseG-factorFusABacterial elongation factor GRibosome-EF-G complex

Inhibition of the translocation step of protein synthesis by stabilizing the EF-G-GDP complex on the ribosome or preventing EF-G binding to the ribosomal A-site.