4.8 Article

Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases

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NATURE COMMUNICATIONS
卷 5, 期 -, 页码 -

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NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms6141

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  1. Commissariat a l'Energie Atomique et aux Energies Alternatives (CEA)
  2. French National Research Agency [ANR 2010/Blan 1501 01]

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Cyclodipeptide synthases form cyclodipeptides from two aminoacyl transfer RNAs. They use a ping-pong mechanism that begins with transfer of the aminoacyl moiety of the first aminoacyl tRNA onto a conserved serine, yielding an aminoacyl enzyme. Combining X-ray crystallography, site-directed mutagenesis and affinity labelling of the cyclodipeptide synthase AlbC, we demonstrate that the covalent intermediate reacts with the aminoacyl moiety of the second aminoacyl tRNA, forming a dipeptidyl enzyme, and identify the aminoacyl-binding sites of the aminoacyl tRNAs.

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