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2z3m

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[[Image:2z3m.gif|left|200px]]<br /><applet load="2z3m" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2z3m.gif|left|200px]]
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caption="2z3m, resolution 2.70&Aring;" />
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'''complex structure of LF-transferase and dAF'''<br />
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{{Structure
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|PDB= 2z3m |SIZE=350|CAPTION= <scene name='initialview01'>2z3m</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=3D1:5-(6-AMINO-PURIN-9-YL)-2-HYDROXYMETHYL-TETRAHYDRO-FURAN-3-OL'>3D1</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene> and <scene name='pdbligand=TAR:D(-)-TARTARIC ACID'>TAR</scene>
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|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]
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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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'''complex structure of LF-transferase and dAF'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2Z3M 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=3D1:'>3D1</scene>, <scene name='pdbligand=PHE:'>PHE</scene> and <scene name='pdbligand=TAR:'>TAR</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=2Z3M OCA].
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2Z3M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z3M OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17891155 17891155]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17891155 17891155]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Leucyltransferase]]
[[Category: Leucyltransferase]]
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[[Category: lf-transferase]]
[[Category: lf-transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:59:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:51:49 2008''

Revision as of 16:51, 20 March 2008

Image:2z3m.gif


PDB ID 2z3m

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: , and
Gene: Aat (Escherichia coli)
Activity: Leucyltransferase, with EC number 2.3.2.6
Coordinates: save as pdb, mmCIF, xml



complex structure of LF-transferase and dAF


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

2Z3M 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

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