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

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 mutagenes...

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Published inNature communications Vol. 5; no. 1; p. 5141
Main Authors Moutiez, Mireille, Schmitt, Emmanuelle, Seguin, Jérôme, Thai, Robert, Favry, Emmanuel, Belin, Pascal, Mechulam, Yves, Gondry, Muriel
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 06.10.2014
Subjects
Bacterial Proteins - chemistry
Biochemistry, Molecular Biology
Catalysis
Catalytic Domain
Crystallography, X-Ray
Life Sciences
Molecular Conformation
Mutagenesis, Site-Directed
Peptide Biosynthesis
Peptide Synthases - chemistry
Ribosomes - chemistry
RNA, Transfer - chemistry
Serine - chemistry
Streptomyces - chemistry
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Summary: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.
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms6141