Elongation factor P

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Elongation factor P (EF-P) KOW-like domain
PDB 1iz6 EBI.jpg
crystal structure of translation initiation factor 5a from pyrococcus horikoshii
Identifiers
Symbol EFP_N
Pfam PF08207
Pfam clan CL0107
InterPro IPR013185
PROSITE PDOC00981
Elongation factor P (EF-P) OB domain
PDB 1ueb EBI.jpg
crystal structure of translation elongation factor p from thermus thermophilus hb8
Identifiers
Symbol EFP
Pfam PF01132
Pfam clan CL0021
InterPro IPR001059
PROSITE PDOC00981
CDD cd04470
Elongation factor P, C-terminal
PDB 1ueb EBI.jpg
crystal structure of translation elongation factor p from thermus thermophilus hb8
Identifiers
Symbol Elong-fact-P_C
Pfam PF09285
InterPro IPR015365
SCOP 1ueb
SUPERFAMILY 1ueb
CDD cd05794

EF-P (elongation factor P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet.[1] 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[2]
  • A C-terminal domain which adopts an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology[2]

eIF5A is the eukaryotic homolog of EF-P.

Function[edit]

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.[3] Additionally, EF-P has been shown to assist in efficient translation of three or more consecutive proline residues.[4]

See also[edit]

References[edit]

  1. ^ Aoki H, Adams SL, Turner MA, Ganoza MC (1997). "Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction". Biochimie. 79 (1): 7–11. doi:10.1016/S0300-9084(97)87619-5. PMID 9195040. 
  2. ^ a b Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S (June 2004). "Crystal structure of elongation factor P from Thermus thermophilus HB8". Proc. Natl. Acad. Sci. U.S.A. 101 (26): 9595–600. doi:10.1073/pnas.0308667101. PMC 470720Freely accessible. PMID 15210970. 
  3. ^ Leaps in Translational Elongation Science (2009) 326, 677.
  4. ^ Ude, Susanne; Lassak, Jürgen; Starosta, Agata L.; Kraxenberger, Tobias; Wilson, Daniel N.; Jung, Kirsten (2013-01-04). "Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches". Science. 339 (6115): 82–85. doi:10.1126/science.1228985. ISSN 0036-8075. PMID 23239623. 
This article incorporates text from the public domain Pfam and InterPro: IPR001059
This article incorporates text from the public domain Pfam and InterPro: IPR015365