| dbo:abstract |
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) |
| dbo:symbol |
EFP EFP_N Elong-fact-P_C |
| dbo:thumbnail |
wiki-commons:Special:FilePath/PDB_1iz6_EBI.jpg?width=300 |
| dbo:wikiPageID |
32678860 (xsd:integer) |
| dbo:wikiPageLength |
11459 (xsd:nonNegativeInteger) |
| dbo:wikiPageRevisionID |
1092907656 (xsd:integer) |
| dbo:wikiPageWikiLink |
dbr:Aminoacyl-tRNA dbr:Puromycin dbr:Hypusine dbr:Peptide_bonds dbr:EF-G dbr:EF-Tu dbr:EIF5A dbr:Nucleic_acid dbr:Protein_domains dbr:Protein_synthesis dbr:Anticodon dbr:Bacteria dbr:GTPase dbr:EF-Ts dbr:Binding_(molecular) dbr:Protein dbc:Protein_domains dbr:Termination_factor dbr:Translation_(biology) dbr:Proteinogenic_amino_acid dbr:Prokaryotic_elongation_factors dbr:Initiation_factors dbr:Peptidyl_transferase dbr:Ribosomes dbr:TRNA dbr:P_site dbr:Elongation_factors dbr:EIF-5A dbr:E_site dbr:Beta-barrel |
| dbp:caption |
crystal structure of translation elongation factor p from thermus thermophilus hb8 (en) crystal structure of translation initiation factor 5a from pyrococcus horikoshii (en) |
| dbp:cdd |
cd04470 (en) cd05794 (en) |
| dbp:interpro |
IPR001059 (en) IPR013185 (en) IPR015365 (en) |
| dbp:name |
Elongation factor P KOW-like domain (en) Elongation factor P OB domain (en) Elongation factor P, C-terminal (en) |
| dbp:pfam |
PF01132 (en) PF08207 (en) PF09285 (en) |
| dbp:pfamClan |
CL0021 (en) CL0107 (en) |
| dbp:prosite |
PDOC00981 (en) |
| dbp:scop |
1 (xsd:integer) |
| dbp:symbol |
EFP (en) EFP_N (en) Elong-fact-P_C (en) |
| dbp:wikiPageUsesTemplate |
dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist dbt:Genetic_translation |
| dct:subject |
dbc:Protein_domains |
| gold:hypernym |
dbr:Factor |
| rdf:type |
owl:Thing dbo:Biomolecule wikidata:Q206229 wikidata:Q8054 yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity dbo:Protein yago:SocialGroup107950920 yago:Unit108189659 |
| rdfs:comment |
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) |
| rdfs:label |
Elongation factor P (en) |
| owl:sameAs |
freebase:Elongation factor P wikidata:Elongation factor P https://global.dbpedia.org/id/4k5f8 |
| prov:wasDerivedFrom |
wikipedia-en:Elongation_factor_P?oldid=1092907656&ns=0 |
| foaf:depiction |
wiki-commons:Special:FilePath/PDB_1iz6_EBI.jpg wiki-commons:Special:FilePath/PDB_1ueb_EBI.jpg |
| foaf:isPrimaryTopicOf |
wikipedia-en:Elongation_factor_P |
| is dbo:wikiPageDisambiguates of |
dbr:EFP |
| is dbo:wikiPageWikiLink of |
dbr:Archaeal_initiation_factors dbr:EF-G dbr:EF-Tu dbr:EIF5A dbr:Initiation_factor dbr:Elongation_factor dbr:Post-translational_modification dbr:2-Aminoisobutyric_acid dbr:EF-Ts dbr:EFP dbr:Eukaryotic_initiation_factor dbr:Ribosomal_pause |
| is foaf:primaryTopic of |
wikipedia-en:Elongation_factor_P |
