2z3p
From Proteopedia
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|PDB= 2z3p |SIZE=350|CAPTION= <scene name='initialview01'>2z3p</scene>, resolution 2.50Å | |PDB= 2z3p |SIZE=350|CAPTION= <scene name='initialview01'>2z3p</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> | + | |LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</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= Aat ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= Aat ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2z3k|2Z3K]], [[2z3l|2Z3L]], [[2z3m|2Z3M]], [[2z3n|2Z3N]], [[2z3o|2Z3O]] | ||
| + | |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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[[Category: Tomita, K.]] | [[Category: Tomita, K.]] | ||
[[Category: Watanabe, K.]] | [[Category: Watanabe, K.]] | ||
| - | [[Category: LEU]] | ||
| - | [[Category: TAR]] | ||
[[Category: lf-transferase]] | [[Category: lf-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 05:18:16 2008'' |
Revision as of 02:18, 31 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | Aat (Escherichia coli) | ||||||
| Activity: | Leucyltransferase, with EC number 2.3.2.6 | ||||||
| Related: | 2Z3K, 2Z3L, 2Z3M, 2Z3N, 2Z3O
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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