page_title: Elongation factor P
hierarchical_section_title: Elongation factor P
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 1ueb code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 1ueb code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 1ueb registreert is.
context_page_description: EF-P is an essential protein that in eubacteria stimulates the formation of the first peptide bonds in protein synthesis. Studies show that EF-P prevents ribosomes from stalling during the synthesis of proteins containing consecutive prolines. EF-P binds to a site located between the binding site for the peptidyl tRNA and the exiting tRNA. It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. The EF-P protein shape and size is very similar to a tRNA and interacts with the ribosome via the exit “E” site on the 30S subunit and the peptidyl-transferase center of the 50S subunit. EF-P is a translation aspect of an unknown function, therefore It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
  EF-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
context_section_description: EF-P (elongation factor P) is an essential protein that in eubacteria stimulates the formation of the first peptide bonds in protein synthesis. Studies show that EF-P prevents ribosomes from stalling during the synthesis of proteins containing consecutive prolines. EF-P binds to a site located between the binding site for the peptidyl tRNA (P site) and the exiting tRNA (E site). It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. The EF-P protein shape and size is very similar to a tRNA and interacts with the ribosome via the exit “E” site on the 30S subunit and the peptidyl-transferase center (PTC) of the 50S subunit. EF-P is a translation aspect of an unknown function, therefore It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
  EF-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
  Eukaryotes and archaebacteria lack EF-P. In eukaryotes, a similar function is performed by the eukaryotic initiation factor, eIF-5A, which exhibits some modest sequence and structural similarity with EF-P. There are, however, many difference differences between EF-p and eIF-5A. EF-P has a structure similar to that of L-shaped tRNA and it contains three (I,II and III) β-barrel domains. In contrast, eIF-5A contains only two domains (C and N). Moreover, as opposed to eIF-5A, which contains the non-proteinogenic amino acid hypusine that is essential for its activity, EF-P undergoes no post-translational amino acid modifications. Finally EF-P is about 40 amino acids longer than shorter than eIF-5A.
caption: crystal structure of translation elongation factor p from thermus thermophilus hb8
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