Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
Autor: | Kozo Tomita, Kyoko Suto, Shuya Fukai, Kazunori Watanabe, Takuya Ueda, Osamu Nureki, Yoshihiro Shimizu |
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Rok vydání: | 2006 |
Předmět: |
Models
Molecular Molecular Sequence Data RNA Transfer Amino Acyl Protein degradation Biology Arginine Crystallography X-Ray Protein Structure Secondary Article General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Protein structure Escherichia coli Transferase Amino Acid Sequence Molecular Biology Aminoacyl-tRNA General Immunology and Microbiology Escherichia coli Proteins Lysine General Neuroscience Aminoacyltransferases chemistry Biochemistry Structural Homology Protein Puromycin Acetyltransferase Transfer RNA Mutant Proteins Leucine |
Zdroj: | The EMBO Journal. 25:5942-5950 |
ISSN: | 1460-2075 0261-4189 |
DOI: | 10.1038/sj.emboj.7601433 |
Popis: | 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. |
Databáze: | OpenAIRE |
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