Summary: Elongation factor P, C-terminal
This is the Wikipedia entry entitled "Elongation factor P". More...
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Elongation factor P Edit Wikipedia article
|Elongation factor P (EF-P) KOW-like domain|
crystal structure of translation initiation factor 5a from pyrococcus horikoshii
|Elongation factor P (EF-P) OB domain|
crystal structure of translation elongation factor p from thermus thermophilus hb8
|Elongation factor P, C-terminal|
crystal structure of translation elongation factor p from thermus thermophilus hb8
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:
- 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
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.
- 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.
- 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 470720. PMID 15210970.
- Leaps in Translational Elongation Science (2009) 326, 677.
Elongation factor P, C-terminal Provide feedback
Members of this family of nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology .
Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S; , Proc Natl Acad Sci U S A. 2004;101:9595-9600.: Crystal structure of elongation factor P from Thermus thermophilus HB8. PUBMED:15210970 EPMC:15210970
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015365
These nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology [PUBMED:15210970].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Biological process||peptide biosynthetic process (GO:0043043)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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EGFdomains, and finally a single
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Curation and family details
|Number in seed:||108|
|Number in full:||5622|
|Average length of the domain:||55.20 aa|
|Average identity of full alignment:||50 %|
|Average coverage of the sequence by the domain:||29.52 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Elong-fact-P_C domain has been found. There are 10 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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