ArticleNucleic acids research2014
Specificity determinants for the two tRNA substrates of the cyclodipeptide synthase AlbC from Streptomyces noursei.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- The tRNA moieties of both aminoacyl-tRNA substrates of a cyclodipeptide synthase share a common binding site, as revealed by RNA microhelices mimicking tRNA acceptor arms.Nucleic acids research · 2026Article
- Biosynthesis of Unnatural Cyclodipeptides through Genetic Code Expansion and Cyclodipeptide Synthase Evolution.Journal of the American Chemical Society · 2025Article
- Crystal Structure and Mutagenesis of an XYP Subfamily Cyclodipeptide Synthase Reveal Key Determinants of Enzyme Activity and Substrate Specificity.Biochemistry · 2024Article
- Cyclodipeptide oxidase is an enzyme filament.Nature communications · 2024Article
- Directed evolution of a cyclodipeptide synthase with new activitiesChemical science · 2022Article
- A [3Fe-4S] cluster and tRNA-dependent aminoacyltransferase BlsK in the biosynthesis of Blasticidin S.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme.RSC chemical biology · 2021Article
- Flexizyme-aminoacylated shortened tRNAs demonstrate that only the aminoacylated acceptor arms of the two tRNA substrates are required for cyclodipeptide synthase activity.Nucleic acids research · 2020Article
- Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates.RNA (New York, N.Y.) · 2020Article
- Strategy for the Biosynthesis of Short Oligopeptides: Green and Sustainable Chemistry.Biomolecules · 2019Review
- Genome mining of cyclodipeptide synthases unravels unusual tRNA-dependent diketopiperazine-terpene biosynthetic machinery.Nature communications · 2018Article
- Investigation of Amide Bond Formation during Dehydrophos Biosynthesis.ACS chemical biology · 2018Article
- A Comprehensive Overview of the Cyclodipeptide Synthase Family Enriched with the Characterization of 32 New Enzymes.Frontiers in microbiology · 2018Article
- Cameo appearances of aminoacyl-tRNA in natural product biosynthesis.Current opinion in chemical biology · 2016Review
- Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology.Molecular microbiology · 2016Review
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Structure and tRNA Specificity of MibB, a Lantibiotic Dehydratase from Actinobacteria Involved in NAI-107 Biosynthesis.Cell chemical biology · 2016Article
- Analysis of 51 cyclodipeptide synthases reveals the basis for substrate specificity.Nature chemical biology · 2015Article
- The tRNA-dependent biosynthesis of modified cyclic dipeptides.International journal of molecular sciences · 2014Review
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNA substrates in a sequential ping-pong mechanism to form a cyclodipeptide. The crystal structures of three CDPSs have been determined and all show a Rossmann-fold domain similar to the catalytic domain of class-I aminoacyl-tRNA synthetases (aaRSs). Structural features and mutational analyses however suggest that CDPSs and aaRSs interact differently with their tRNA substrates. We used AlbC from Streptomyces noursei that mainly produces cyclo(l-Phe-l-Leu) to investigate the interaction of a CDPS with its substrates. We demonstrate that Phe-tRNA(Phe) is the first substrate accommodated by AlbC. Its binding to AlbC is dependent on basic residues located in the helix α4 that form a basic patch at the surface of the protein. AlbC does not use all of the Leu-tRNA(Leu) isoacceptors as a second substrate. We show that the G(1)-C(72) pair of the acceptor stem is essential for the recognition of the second substrate. Substitution of D163 located in the loop α6-α7 or D205 located in the loop β6-α8 affected Leu-tRNA(Leu) isoacceptors specificity, suggesting the involvement of these residues in the binding of the second substrate. This is the first demonstration that the two substrates of CDPSs are accommodated in different binding sites.
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