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| {{STRUCTURE_2dps| PDB=2dps | SCENE= }} | | {{STRUCTURE_2dps| PDB=2dps | SCENE= }} |
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| '''Structure of Leucyl/phenylalanyl-tRNA-protein transferase'''
| | ===Structure of Leucyl/phenylalanyl-tRNA-protein transferase=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17110926}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17110926 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17110926}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tomita, K.]] | | [[Category: Tomita, K.]] |
| [[Category: Aminoacyl-trna-protein transferase]] | | [[Category: Aminoacyl-trna-protein transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:56:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:16:25 2008'' |
