2DPT

Leucyl/phenylalanyl-tRNA-protein transferase complexed with puromycin

Summary for 2DPT

• Entry DOI: 10.2210/pdb2dpt/pdb
• Related: 2DPS
• Descriptor: Leucyl/phenylalanyl-tRNA--protein transferase, PUROMYCIN, D(-)-TARTARIC ACID, ... (4 entities in total)
• Functional Keywords: aminoacyl-trna-protein transferase, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A8P1
• Total number of polymer chains: 2
• Total formula weight: 58888.94

Authors

Suto, K.,Shimizu, Y.,Tomita, K. (deposition date: 2006-05-14, release date: 2007-01-02, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.75 Å)