2DPS

Structure of Leucyl/phenylalanyl-tRNA-protein transferase

2DPS の概要

• エントリーDOI: 10.2210/pdb2dps/pdb
• 関連するPDBエントリー: 2DPT
• 分子名称: Leucyl/phenylalanyl-tRNA--protein transferase (2 entities in total)
• 機能のキーワード: aminoacyl-trna-protein transferase, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A8P1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57645.75

構造登録者

Suto, K.,Shimizu, Y.,Tomita, K. (登録日: 2006-05-14, 公開日: 2007-01-02, 最終更新日: 2024-03-13)

主引用文献

Suto, K.,Shimizu, Y.,Watanabe, K.,Ueda, T.,Fukai, S.,Nureki, O.,Tomita, K.
Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
Embo J., 25:5942-5950, 2006

PubMed Abstract: 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), is accommodated in a highly hydrophobic pocket, with a shape and size suitable for hydrophobic amino-acid residues lacking a branched beta-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.

PubMed: 17110926
DOI: 10.1038/sj.emboj.7601433

実験手法

X-RAY DIFFRACTION (2.4 Å)