Elongation factor P

Updated on Jan 12, 2024

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Symbol EFP_N Pfam clan CL0107 PROSITE PDOC00981		Pfam PF08207 InterPro IPR013185 Pfam structures

In molecular biology, elongation factor P is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet. It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.

Elongation factor P consists of three domains:

An N-terminal KOW-like domain

A central OB domain, which forms an oligonucleotide-binding fold. It is not clear if this region is involved in binding nucleic acids

A C-terminal domain which adopts an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology

eIF5A is the eukaryotic homolog of EF-P.

Function

It has been suggested that after binding of the initiator tRNA to the P/I site, it is correctly positioned to the P site by binding of EF-P to the E site.

References

Elongation factor P Wikipedia

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