Bacterial elongation factor G – ribosome complex (EF-G–ribosome complex)

The bacterial elongation factor G (EF-G) – ribosome complex is a fundamental molecular assembly required for the elongation phase of bacterial protein synthesis. EF-G is a translocase enzyme that utilizes GTP hydrolysis to drive the movement of messenger RNA and transfer RNAs through the ribosome (UniProt P0A6M8). This complex is a validated therapeutic target for antibiotics, most notably fusidic acid, which exerts its effect by binding to EF-G after GTP hydrolysis (PubMed 25648508). By stabilizing the EF-G–GDP–ribosome complex, the drug prevents the release of EF-G, effectively stalling the ribosome and halting further protein production. This mechanism is primarily utilized to treat infections caused by Gram-positive bacteria, such as Staphylococcus aureus (StatPearls NBK541058). Understanding the structural dynamics of this complex is crucial for overcoming antibiotic resistance, which often arises from mutations in the fusA gene encoding EF-G (PubMed 12936920).

Other names

EF-G–ribosome complexTranslocase–ribosome complexElongation factor G–70S ribosome complexFusidic acid–EF-G–ribosome complex

Inhibition of bacterial protein synthesis by stabilizing the elongation factor G–GDP–ribosome complex, thereby preventing the dissociation of EF-G and stalling the translocation process.