2dpt
From Proteopedia
(New page: 200px<br /><applet load="2dpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dpt, resolution 2.75Å" /> '''Leucyl/phenylalanyl-...) |
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| - | [[Image:2dpt.jpg|left|200px]]<br /><applet load="2dpt" size=" | + | [[Image:2dpt.jpg|left|200px]]<br /><applet load="2dpt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2dpt, resolution 2.75Å" /> | caption="2dpt, resolution 2.75Å" /> | ||
'''Leucyl/phenylalanyl-tRNA-protein transferase complexed with puromycin'''<br /> | '''Leucyl/phenylalanyl-tRNA-protein transferase complexed with puromycin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Eubacterial leucyl/phenylalanyl-tRNA protein transferase | + | 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== | ==About this Structure== | ||
| - | 2DPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TAR and PUY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Leucyltransferase Leucyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.6 2.3.2.6] Full crystallographic information is available from [http:// | + | 2DPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=TAR:'>TAR</scene> and <scene name='pdbligand=PUY:'>PUY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Leucyltransferase Leucyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.6 2.3.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: aminoacyl-trna-protein transferase]] | [[Category: aminoacyl-trna-protein transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:17 2008'' |
Revision as of 15:01, 21 February 2008
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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 and 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
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