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http://purl.uniprot.org/citations/21296757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21296757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21296757http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/21296757http://www.w3.org/2000/01/rdf-schema#comment"Cyclodipeptide synthases (CDPSs) belong to a newly defined family of enzymes that use aminoacyl-tRNAs (aa-tRNAs) as substrates to synthesize the two peptide bonds of various cyclodipeptides, which are the precursors of many natural products with noteworthy biological activities. Here, we describe the crystal structure of AlbC, a CDPS from Streptomyces noursei. The AlbC structure consists of a monomer containing a Rossmann-fold domain. Strikingly, it is highly similar to the catalytic domain of class-I aminoacyl-tRNA synthetases (aaRSs), especially class-Ic TyrRSs and TrpRSs. AlbC contains a deep pocket, highly conserved among CDPSs. Site-directed mutagenesis studies indicate that this pocket accommodates the aminoacyl moiety of the aa-tRNA substrate in a way similar to that used by TyrRSs to recognize their tyrosine substrates. These studies also suggest that the tRNA moiety of the aa-tRNA interacts with AlbC via at least one patch of basic residues, which is conserved among CDPSs but not present in class-Ic aaRSs. AlbC catalyses its two-substrate reaction via a ping-pong mechanism with a covalent intermediate in which L-Phe is shown to be transferred from Phe-tRNA(Phe) to an active serine. These findings provide insight into the molecular bases of the interactions between CDPSs and their aa-tRNAs substrates, and the catalytic mechanism used by CDPSs to achieve the non-ribosomal synthesis of cyclodipeptides."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkr027"xsd:string
http://purl.uniprot.org/citations/21296757http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkr027"xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Le Du M.H."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Le Du M.H."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Thai R."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Thai R."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Seguin J."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Seguin J."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Gondry M."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Gondry M."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Pernodet J.L."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Pernodet J.L."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Masson C."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Masson C."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Belin P."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Belin P."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Sauguet L."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Sauguet L."xsd:string
http://purl.uniprot.org/citations/21296757http://purl.uniprot.org/core/author"Charbonnier J.B."xsd:string