Elongation factor P
| Elongation factor P (EF-P) KOW-like domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
crystal structure of translation initiation factor 5a from pyrococcus horikoshii
|
|||||||||
| Identifiers | |||||||||
| Symbol | EFP_N | ||||||||
| Pfam | PF08207 | ||||||||
| Pfam clan | CL0107 | ||||||||
| InterPro | IPR013185 | ||||||||
| PROSITE | PDOC00981 | ||||||||
|
|||||||||
| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| Elongation factor P (EF-P) OB domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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 | ||||||||
|
|||||||||
| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| Elongation factor P, C-terminal | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
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 | ||||||||
|
|||||||||
| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
In molecular biology, elongation factor P is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet. It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Elongation factor P consists of three domains:
eIF5A is the eukaryotic homolog of EF-P.
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.
This article incorporates text from the public domain Pfam and InterPro IPR001059
This article incorporates text from the public domain Pfam and InterPro IPR015365
...
Wikipedia