ArticleNature communications2022
Catalytic trajectory of a dimeric nonribosomal peptide synthetase subunit with an inserted epimerase domain.
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 15 papers.
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Who cites it
15 citing papers in PubMed.
- Structural Basis for a Scaffolding Role of the COM Domain in Nonribosomal Peptide Synthetases.Angewandte Chemie (International ed. in English) · 2025Article
- Automated model-free analysis of cryo-EM volume ensembles with SIREn.Structure (London, England : 1993) · 2025Article
- Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.Nature communications · 2025Article
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- Article
- Automated model-free analysis of cryo-EM volume ensembles with SIREn.bioRxiv : the preprint server for biology · 2024Article
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.Science advances · 2024Article
- 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
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- 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
- Structural identification of catalytic His158 of PtMAC2p fromFrontiers in bioengineering and biotechnology · 2023Article
- Exploring the Structural Variability of Dynamic Biological Complexes by Single-Particle Cryo-Electron Microscopy.Micromachines · 2022Review
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Authors and funding
10 authors.
Funding
Abstract
Nonribosomal peptide synthetases (NRPSs) are modular assembly-line megaenzymes that synthesize diverse metabolites with wide-ranging biological activities. The structural dynamics of synthetic elongation has remained unclear. Here, we present cryo-EM structures of PchE, an NRPS elongation module, in distinct conformations. The domain organization reveals a unique "H"-shaped head-to-tail dimeric architecture. The capture of both aryl and peptidyl carrier protein-tethered substrates and intermediates inside the heterocyclization domain and L-cysteinyl adenylate in the adenylation domain illustrates the catalytic and recognition residues. The multilevel structural transitions guided by the adenylation C-terminal subdomain in combination with the inserted epimerase and the conformational changes of the heterocyclization tunnel are controlled by two residues. Moreover, we visualized the direct structural dynamics of the full catalytic cycle from thiolation to epimerization. This study establishes the catalytic trajectory of PchE and sheds light on the rational re-engineering of domain-inserted dimeric NRPSs for the production of novel pharmaceutical agents.
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