2z3p
From Proteopedia
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| - | [[Image:2z3p.gif|left|200px]] | + | [[Image:2z3p.gif|left|200px]] |
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| - | '''complex structure of LF-transferase and leucine''' | + | {{Structure |
| + | |PDB= 2z3p |SIZE=350|CAPTION= <scene name='initialview01'>2z3p</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> and <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] | ||
| + | |GENE= Aat ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''complex structure of LF-transferase and leucine''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2Z3P is a [ | + | 2Z3P 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=2Z3P OCA]. |
==Reference== | ==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:[http:// | + | 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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:51:48 2008'' |
Revision as of 16:51, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 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
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