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

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Moutiez, Mireille | Schmitt, Emmanuelle | Seguin, Jérôme | Thai, Robert | Favry, Emmanuel | Belin, Pascal | Mechulam, Yves | Gondry, Muriel

Edité par CCSD ; Nature Publishing Group -

International audience. 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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