ArticleAngewandte Chemie (International ed. in English)2022
FRET Monitoring of a Nonribosomal Peptide Synthetase Elongation Module Reveals Carrier Protein Shuttling between Catalytic Domains.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- Three-Segment Protein Labeling Using a Highly Efficient and Cysteine-Less Split Intein Identified with Computational Prediction of Aggregation Properties.Angewandte Chemie (International ed. in English) · 2025Article
- Structural Basis for a Scaffolding Role of the COM Domain in Nonribosomal Peptide Synthetases.Angewandte Chemie (International ed. in English) · 2025Article
- A Genetically Encoded Homocysteine Precursor to Probe Protein Active Sites and to Addict Escherichia coli to a Noncanonical Amino Acid Directly Involved in Catalysis.Angewandte Chemie (International ed. in English) · 2025Article
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- Subdomain dynamics enable chemical chain reactions in non-ribosomal peptide synthetases.Nature chemistry · 2024Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Structure modification of an antibiotic: by engineering the fusaricidin bio-synthetase A inFrontiers in microbiology · 2023Article
- FRET Monitoring of a Nonribosomal Peptide Synthetase Elongation Module Reveals Carrier Protein Shuttling between Catalytic Domains.Angewandte Chemie (International ed. in English) · 2022Article
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5 authors.
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Abstract
Nonribosomal peptide synthetases (NRPSs) employ multiple domains, specifically arranged in modules, for the assembly-line biosynthesis of a plethora of bioactive peptides. It is poorly understood how catalysis is correlated with the domain interplay and associated conformational changes. We developed FRET sensors of an elongation module to study in solution the intramodular interactions of the peptidyl carrier protein (PCP) with adenylation (A) and condensation (C) domains. Backed by HDX-MS analysis, we discovered dynamic mixtures of conformations that undergo distinct population changes in favor of the PCP-A and PCP-C interactions upon completion of the adenylation and thiolation reactions, respectively. To probe this model we blocked PCP binding to the C domain by photocaging and triggered peptide bond formation with light. Changing intramodular domain affinities of the PCP appear to result in conformational shifts according to the logic of the templated assembly process.
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