2dpt
From Proteopedia
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|PDB= 2dpt |SIZE=350|CAPTION= <scene name='initialview01'>2dpt</scene>, resolution 2.75Å | |PDB= 2dpt |SIZE=350|CAPTION= <scene name='initialview01'>2dpt</scene>, resolution 2.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=PUY:PUROMYCIN'>PUY</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2dps|2DPS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpt OCA], [http://www.ebi.ac.uk/pdbsum/2dpt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpt RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Suto, K.]] | [[Category: Suto, K.]] | ||
[[Category: Tomita, K.]] | [[Category: Tomita, K.]] | ||
| - | [[Category: PUY]] | ||
| - | [[Category: TAR]] | ||
[[Category: aminoacyl-trna-protein transferase]] | [[Category: aminoacyl-trna-protein transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:49 2008'' |
Revision as of 23:37, 30 March 2008
| |||||||
| , resolution 2.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Leucyltransferase, with EC number 2.3.2.6 | ||||||
| Related: | 2DPS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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