論文

査読有り
2007年10月

Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase

NATURE
  • Kazunori Watanabe
  • ,
  • Yukimatsu Toh
  • ,
  • Kyoko Suto
  • ,
  • Yoshihiro Shimizu
  • ,
  • Natsuhisa Oka
  • ,
  • Takeshi Wada
  • ,
  • Kozo Tomita

449
7164
開始ページ
867
終了ページ
U5
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/nature06167
出版者・発行元
NATURE PUBLISHING GROUP

Eubacterial leucyl/phenylalanyl-tRNA protein transferase (LF-transferase) catalyses peptide-bond formation by using Leu-tRNA(Leu) (or Phe-tRNA(Phe)) and an amino-terminal Arg (or Lys) of a protein, as donor and acceptor substrates, respectively. However, the catalytic mechanism of peptide-bond formation by LF-transferase remained obscure. Here we determine the structures of complexes of LF-transferase and phenylalanyl adenosine, with and without a short peptide bearing an N-terminal Arg. Combining the two separate structures into one structure as well as mutation studies reveal the mechanism for peptide-bond formation by LF-transferase. The electron relay from Asp 186 to Gln 188 helps Gln 188 to attract a proton from the alpha-amino group of the N-terminal Arg of the acceptor peptide. This generates the attacking nucleophile for the carbonyl carbon of the aminoacyl bond of the aminoacyl-tRNA, thus facilitating peptide-bond formation. The protein-based mechanism for peptide-bond formation by LF-transferase is similar to the reverse reaction of the acylation step observed in the peptide hydrolysis reaction by serine proteases.

Web of Science ® 被引用回数 : 61

リンク情報
DOI
https://doi.org/10.1038/nature06167
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000250230600038&DestApp=WOS_CPL

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