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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. ==Function== 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.〔 Leaps in Translational Elongation (Science (2009) 326, 677 ).〕 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Elongation factor P」の詳細全文を読む スポンサード リンク
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