Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis.
作者： Ludovic Sauguet , Mireille Moutiez , Yan Li , Pascal Belin , Jérôme Seguin
DOI: 10.1093/NAR/GKR027
关键词:
摘要: Cyclodipeptide synthases (CDPSs) belong to a newly defined family of enzymes that use aminoacyl-tRNAs (aa-tRNAs) as substrates synthesize the two peptide bonds various cyclodipeptides, which are precursors many natural products with noteworthy biological activities. Here, we describe crystal structure AlbC, CDPS from Streptomyces noursei. The AlbC consists monomer containing Rossmann-fold domain. Strikingly, it is highly similar catalytic domain class-I aminoacyl-tRNA synthetases (aaRSs), especially class-Ic TyrRSs and TrpRSs. contains deep pocket, conserved among CDPSs. Site-directed mutagenesis studies indicate this pocket accommodates aminoacyl moiety aa-tRNA substrate in way used by recognize their tyrosine substrates. These also suggest tRNA interacts via at least one patch basic residues, CDPSs but not present aaRSs. catalyses its two-substrate reaction ping-pong mechanism covalent intermediate L-Phe shown be transferred Phe-tRNA(Phe) an active serine. findings provide insight into molecular bases interactions between aa-tRNAs substrates, achieve non-ribosomal synthesis cyclodipeptides.
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