2dpt
From Proteopedia
|
Leucyl/phenylalanyl-tRNA-protein transferase complexed with puromycin
Overview
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.
About this Structure
2DPT is a Single protein structure of sequence from Escherichia coli with TAR and PUY as ligands. Active as Leucyltransferase, with EC number 2.3.2.6 Full crystallographic information is available from OCA.
Reference
Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog., Suto K, Shimizu Y, Watanabe K, Ueda T, Fukai S, Nureki O, Tomita K, EMBO J. 2006 Dec 13;25(24):5942-50. Epub 2006 Nov 16. PMID:17110926
Page seeded by OCA on Wed Nov 21 09:42:50 2007
