2z3p

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[[Image:2z3p.gif|left|200px]]
[[Image:2z3p.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2z3p |SIZE=350|CAPTION= <scene name='initialview01'>2z3p</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2z3p", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= Aat ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_2z3p| PDB=2z3p | SCENE= }}
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|RELATEDENTRY=[[2z3k|2Z3K]], [[2z3l|2Z3L]], [[2z3m|2Z3M]], [[2z3n|2Z3N]], [[2z3o|2Z3O]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z3p OCA], [http://www.ebi.ac.uk/pdbsum/2z3p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2z3p RCSB]</span>
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}}
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'''complex structure of LF-transferase and leucine'''
'''complex structure of LF-transferase and leucine'''
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[[Category: Tomita, K.]]
[[Category: Tomita, K.]]
[[Category: Watanabe, K.]]
[[Category: Watanabe, K.]]
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[[Category: lf-transferase]]
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[[Category: Lf-transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:55:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:18:16 2008''
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Revision as of 16:55, 4 May 2008

Image:2z3p.gif

Template:STRUCTURE 2z3p

complex structure of LF-transferase and leucine


Overview

Eubacterial leucyl/phenylalanyl-tRNA protein transferase (LF-transferase) catalyses peptide-bond formation by using Leu-tRNA(Leu) (or Phe-tRNA(Phe)) and an amino-terminal Arg (or Lys) of a protein, as donor and acceptor substrates, respectively. However, the catalytic mechanism of peptide-bond formation by LF-transferase remained obscure. Here we determine the structures of complexes of LF-transferase and phenylalanyl adenosine, with and without a short peptide bearing an N-terminal Arg. Combining the two separate structures into one structure as well as mutation studies reveal the mechanism for peptide-bond formation by LF-transferase. The electron relay from Asp 186 to Gln 188 helps Gln 188 to attract a proton from the alpha-amino group of the N-terminal Arg of the acceptor peptide. This generates the attacking nucleophile for the carbonyl carbon of the aminoacyl bond of the aminoacyl-tRNA, thus facilitating peptide-bond formation. The protein-based mechanism for peptide-bond formation by LF-transferase is similar to the reverse reaction of the acylation step observed in the peptide hydrolysis reaction by serine proteases.

About this Structure

2Z3P is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase., Watanabe K, Toh Y, Suto K, Shimizu Y, Oka N, Wada T, Tomita K, Nature. 2007 Oct 18;449(7164):867-71. Epub 2007 Sep 23. PMID:17891155 Page seeded by OCA on Sun May 4 19:55:28 2008

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