| dbo:abstract
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- EF-P (elongation factor P) is an essential protein that in bacteria 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 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. 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. (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). (en)
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- 11459 (xsd:nonNegativeInteger)
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- crystal structure of translation elongation factor p from thermus thermophilus hb8 (en)
- crystal structure of translation initiation factor 5a from pyrococcus horikoshii (en)
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| dbp:cdd
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- cd04470 (en)
- cd05794 (en)
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| dbp:interpro
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- IPR001059 (en)
- IPR013185 (en)
- IPR015365 (en)
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| dbp:name
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- Elongation factor P KOW-like domain (en)
- Elongation factor P OB domain (en)
- Elongation factor P, C-terminal (en)
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| dbp:pfam
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- PF01132 (en)
- PF08207 (en)
- PF09285 (en)
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- EFP (en)
- EFP_N (en)
- Elong-fact-P_C (en)
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| rdfs:comment
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- EF-P (elongation factor P) is an essential protein that in bacteria 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. (en)
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