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

Mireille Moutiez 1 Emmanuelle Schmitt 2 Jérôme Seguin 1 Robert Thai 1 Emmanuel Favry 1 Pascal Belin 1 Yves Mechulam 2 Muriel Gondry 1
1 Service d’Ingénierie Moléculaire des Protéines
2 BIOC - Laboratoire de Biochimie de l'Ecole polytechnique
Abstract : 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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Mireille Moutiez, Emmanuelle Schmitt, Jérôme Seguin, Robert Thai, Emmanuel Favry, et al.. Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases.. Nature Communications, Nature Publishing Group, 2014, 5 (October), pp.5141. ⟨10.1038/ncomms6141⟩. ⟨hal-01098814⟩

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