Elongation factor P

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Elongation factor P (EF-P) KOW-like domain
crystal structure of translation initiation factor 5a from pyrococcus horikoshii
Identifiers
SymbolEFP_N
PfamPF08207
Pfam clanCL0107
InterProIPR013185
PROSITEPDOC00981
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Elongation factor P (EF-P) OB domain
crystal structure of translation elongation factor p from thermus thermophilus hb8
Identifiers
SymbolEFP
PfamPF01132
Pfam clanCL0021
InterProIPR001059
PROSITEPDOC00981
CDDcd04470
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Elongation factor P, C-terminal
SCOP2
1ueb / SCOPe / SUPFAM
CDDcd05794
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

EF-P (elongation factor P) is an essential

anticodon stem-loop of the P site-bound initiator tRNA.[3] 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.[4] EF-P is a translation aspect of an unknown function,[1] 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
:

Eukaryotes and archaea lack EF-P. In these domains, a similar function is performed by the archaeo-eukaryotic initiation factor,

a/eIF-5A, which exhibits some modest sequence and structural similarity with EF-P.[2][6] There are, however, important differences between EF-p and eIF-5A. (a) 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) with a corresponding size difference.[2] (b) Moreover, as opposed to eIF-5A, which contains the non-proteinogenic amino acid hypusine that is essential for its activity, EF-P displays a diversity of post-transcriptional modifications at the analogous position (β-lysylation of lysine residue, rhamnosylation of arginine residue, or none at all).[7][8]

Function

In eubacteria, there are three groups of factors that promote protein synthesis:

elongation factors and termination factors.[7] The elongation phase of translation is promoted by three universal elongation factors, EF-Tu, EF-Ts, and EF-G.[9] EF-P was discovered in 1975 by Glick and Ganoza,[10] as a factor that increased the yield of peptide bond formation between initiator fMet-tRNA(fMet) and a mimic of aa-tRNA, puromycin
(Pmn). The low yield of product formation in absence of EF-P can be described by the loss of peptidyl-tRNA from the stalled ribosome. Thus, EF-P is not a necessary component of minimal in vitro translation system, however, the absence of EF-P can limit translation rate, increase antibiotic sensitivity, and slow growth.

To complete its function, EF-P enters paused ribosomes through the E-site and facilitates peptide bond formation through interactions with the P-site tRNA.[11] EF-P and eIF-5A both are essential for the synthesis of a subset of proteins containing proline stretches in all cells.[1]

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.[12] Additionally, EF-P has been shown to assist in efficient translation of three or more consecutive proline residues.[13]

Structure

EF-P is a 21 kDa protein encoded by the efp gene.[9] EF-P consists of three β-barrel domains (I,II and III) and has a L shape tRNA structure. Domain II and III of EF-P are similar to each other. Despite the structural similarity of EF-P with tRNA, studies showed that EF-P does not bind to the ribosome at the classical tRNA binding site, but at the distinct position that is located between the P and E sites.[3]

See also

References

  1. ^
    S2CID 20153355
    .
  2. ^
    PMID 15210970
    .
  3. ^
    PMID 19696344
    .
  4. PMID 25144653
    .
  5. ^
    PMID 15210970
    .
  6. S2CID 25447826
    .
  7. ^
    PMID 22128152
    .
  8. PMID 31178848
    .
  9. ^
    PMID 23828669
    .
  10. PMID 1105576
    .
  11. PMID 30297417
    .
  12. S2CID 45692923
    .
  13. S2CID 206544633
    .
This article incorporates text from the public domain Pfam and InterPro: IPR015365
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