InterPro domain: IPR015365

Elongation factor P (EF-P) stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis [ 1 , 2 , 3 , 4 ]. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This entry includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. These domains adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology [ 5 ].

1. The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis. J. Biol. Chem. 272, 32254-9
2. Characterization of a high-throughput screening assay for inhibitors of elongation factor p and ribosomal peptidyl transferase activity. J Biomol Screen 11, 736-42
3. Elongation factors on the ribosome. Curr. Opin. Struct. Biol. 15, 349-54
4. Elongation factors in protein biosynthesis. Trends Biochem. Sci. 28, 434-41
5. Crystal structure of elongation factor P from Thermus thermophilus HB8. Proc. Natl. Acad. Sci. U.S.A. 101, 9595-600