ArticleNature communications2022
Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Photoreactive Pantetheinyl Mimics Reveal Design Limitations for Crypto-Acyl Carrier Proteins.Chembiochem : a European journal of chemical biology · 2026Article
- Balgacyclamide A: Structural Revision of the First Reported Total Synthesis and Evaluation of Oxazoline Synthesis via β-Hydroxy Amides Dehydrative Cyclization Conditions.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- A Novel Indigoidine-like NRPS Gene fromAntioxidants (Basel, Switzerland) · 2026Article
- Molecular basis for depsipeptide HDAC inhibitor combinatorial biosynthesis.Nature communications · 2026Article
- A Streamlined Synthesis of Adenosine Vinylsulfonamide Probes for Aminoacyl-AMP Mimicry in NRPS.Chembiochem : a European journal of chemical biology · 2026Article
- The Potential of Non-Ribosomal Peptide Engineering for Creating New Antimicrobial Complexes.Molecules (Basel, Switzerland) · 2026Review
- Bacterial secondary metabolites as resistance-modifying adjuvants: microbial origins, molecular mechanisms, and translational relevance.Frontiers in microbiology · 2026Review
- Switching the strict substrate specificities of the β-ketoacyl-acyl carrier protein synthases, FabH and BioZ.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural Basis for a Scaffolding Role of the COM Domain in Nonribosomal Peptide Synthetases.Angewandte Chemie (International ed. in English) · 2025Article
- Whole-Genome Sequencing and Biosynthetic Gene Cluster Analysis of Novel Entomopathogenic BacteriaBiology · 2025Article
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- Cyclodipeptide oxidase is an enzyme filament.Nature communications · 2024Article
- Evolutionary Spread of Distinct O-methyltransferases Guides the Discovery of Unique Isoaspartate-Containing Peptides, Pamtides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Dynamics and mechanistic interpretations of nonribosomal peptide synthetase cyclization domains.Current opinion in chemical biology · 2023Review
- Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Bacillamide F, Extracted from MarineBiology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nonribosomal peptide synthetases (NRPSs) are large modular enzymes that synthesize secondary metabolites and natural product therapeutics. Most NRPS biosynthetic pathways include an NRPS and additional proteins that introduce chemical modifications before, during or after assembly-line synthesis. The bacillamide biosynthetic pathway is a common, three-protein system, with a decarboxylase that prepares an NRPS substrate, an NRPS, and an oxidase. Here, the pathway is reconstituted in vitro. The oxidase is shown to perform dehydrogenation of the thiazoline in the peptide intermediate while it is covalently attached to the NRPS, as the penultimate step in bacillamide D synthesis. Structural analysis of the oxidase reveals a dimeric, two-lobed architecture with a remnant RiPP recognition element and a dramatic wrapping loop. The oxidase forms a stable complex with the NRPS and dimerizes it. We visualized co-complexes of the oxidase bound to the elongation module of the NRPS using X-ray crystallography and cryo-EM. The three active sites (for adenylation, condensation/cyclization, and oxidation) form an elegant arc to facilitate substrate delivery. The structures enabled a proof-of-principle bioengineering experiment in which the BmdC oxidase domain is embedded into the NRPS.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.