論文

査読有り
2006年12月

Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog

EMBO JOURNAL
  • Kyoko Suto
  • ,
  • Yoshihiro Shimizu
  • ,
  • Kazunori Watanabe
  • ,
  • Takuya Ueda
  • ,
  • Shuya Fukai
  • ,
  • Osamu Nureki
  • ,
  • Kozo Tomita

25
24
開始ページ
5942
終了ページ
5950
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/sj.emboj.7601433
出版者・発行元
NATURE PUBLISHING GROUP

Eubacterial leucyl/phenylalanyl-tRNA protein transferase (L/F- transferase), encoded by the aat gene, conjugates leucine or phenylalanine to the N-terminal Arg or Lys residue of proteins, using Leu-tRNA Leu or Phe-tRNA Phe as a substrate. The resulting N-terminal Leu or Phe acts as a degradation signal for the ClpS-ClpAP-mediated N-end rule protein degradation pathway. Here, we present the crystal structures of Escherichia coli L/F-transferase and its complex with an aminoacyl-tRNA analog, puromycin. The C-terminal domain of L/F-transferase consists of the GCN5-related N-acetyltransferase fold, commonly observed in the acetyltransferase superfamily. The p-methoxybenzyl group of puromycin, corresponding to the side chain of Leu or Phe of Leu-tRNA(Leu) or Phe-tRNA(Phe), as accommodated in a highly hydrophobic pocket, with a shape and size suitable for hydrophobic amino-acid residues lacking a branched b-carbon, such as leucine and phenylalanine. Structure-based mutagenesis of L/F-transferase revealed its substrate specificity. Furthermore, we present a model of the L/F-transferase complex with tRNA and substrate proteins bearing an N-terminal Arg or Lys.

Web of Science ® 被引用回数 : 44

リンク情報
DOI
https://doi.org/10.1038/sj.emboj.7601433
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000242891100029&DestApp=WOS_CPL

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