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| [[Image:2z3m.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2z3m| PDB=2z3m | SCENE= }} | | {{STRUCTURE_2z3m| PDB=2z3m | SCENE= }} |
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| '''complex structure of LF-transferase and dAF'''
| | ===complex structure of LF-transferase and dAF=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17891155}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17891155 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17891155}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Watanabe, K.]] | | [[Category: Watanabe, K.]] |
| [[Category: Lf-transferase]] | | [[Category: Lf-transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:55:13 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:43:31 2008'' |
