2dps
From Proteopedia
(New page: 200px<br /><applet load="2dps" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dps, resolution 2.40Å" /> '''Structure of Leucyl/...) |
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| - | [[Image:2dps.jpg|left|200px]]<br /><applet load="2dps" size=" | + | [[Image:2dps.jpg|left|200px]]<br /><applet load="2dps" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2dps, resolution 2.40Å" /> | caption="2dps, resolution 2.40Å" /> | ||
'''Structure of Leucyl/phenylalanyl-tRNA-protein transferase'''<br /> | '''Structure of Leucyl/phenylalanyl-tRNA-protein transferase'''<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== | ||
| - | 2DPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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:// | + | 2DPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=2DPS 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 17:01:26 2008'' |
Revision as of 15:01, 21 February 2008
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Structure of Leucyl/phenylalanyl-tRNA-protein transferase
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
2DPS is a Single protein structure of sequence from Escherichia coli. 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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