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.
Document type :
Journal articles
Complete list of metadatas

Cited literature [29 references]  Display  Hide  Download
https://hal-polytechnique.archives-ouvertes.fr/hal-01098814
Contributor : Denis Roura <>
Submitted on : Monday, November 2, 2015 - 5:27:13 PM
Last modification on : Wednesday, March 27, 2019 - 3:56:02 PM
Long-term archiving on: Friday, April 28, 2017 - 6:10:54 AM

Files

ncomms6141 (1).pdf
Publisher files allowed on an open archive

Identifiers

Collections

CNRS | X | X-BIOCH | CEA | PARISTECH | X-DEP-BIO

Citation

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⟩

Export

BibTeX TEI DC DCterms EndNote

Share

Metrics

Record views

280

Files downloads

471

Contact

Informations

CCSD