Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases. - Archive ouverte HAL Access content directly
Journal Articles Nature Communications Year : 2014

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

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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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hal-01098814 , version 1 (02-11-2015)

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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, 2014, 5 (October), pp.5141. ⟨10.1038/ncomms6141⟩. ⟨hal-01098814⟩
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