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News | Structural biology | Cellular mechanisms
Teams of IBITECS and Ecole Polytechnique (Palaiseau) have deciphered the mechanism used by the cyclodipeptide synthases (CDPS) to catalyze the formation of peptide bonds.
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.
These results should facilitate the engineering of CDPS in order to produce cyclodipeptides, natural or not, with biological properties of interest.
Moutiez M., Schmitt E., Seguin J., Thai R., Favry E., Belin P., Mechulam Y., Gondry M. (2014). Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases. Nat. Commun. (2014) 5:5141 http://dx.doi.org/10.1038/ncomms6141
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