ArticleNature communications2021
Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Reprogramming the enduracidin NRPS assembly line via thioesterase domain relocation.Synthetic and systems biotechnology · 2027Article
- Mapping the nonribosomal specificity code through promiscuity-guided A-domain engineering.Chemical science · 2026Article
- The Potential of Non-Ribosomal Peptide Engineering for Creating New Antimicrobial Complexes.Molecules (Basel, Switzerland) · 2026Review
- Biosynthesis of Antituberculosis Antibiotic Capreomycin Involves aOrganic letters · 2025Article
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- Paving the way for new antimicrobial peptides through molecular de-extinction.Microbial cell (Graz, Austria) · 2025Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- Computational Insights into Amide Bond Formation Catalyzed by the Condensation Domain of Nonribosomal Peptide Synthetases.ACS omega · 2024Article
- Controlling Substrate- and Stereospecificity of Condensation Domains in Nonribosomal Peptide Synthetases.ACS chemical biology · 2024Article
- Biosynthesis of the fungal nonribosomal peptide penilumamide A and biochemical characterization of a pterin-specific adenylation domain.RSC chemical biology · 2023Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Stereomeric Lipopeptides from a Single Non-Ribosomal Peptide Synthetase as an Additional Source of Structural and Functional Diversification inInternational journal of molecular sciences · 2023Article
- P450-mediated dehydrotyrosine formation during WS9326 biosynthesis proceedsActa pharmaceutica Sinica. B · 2023Article
- Advances in the adenylation domain: discovery of diverse non-ribosomal peptides.Applied microbiology and biotechnology · 2023Review
- Knowledge-guided data mining on the standardized architecture of NRPS: Subtypes, novel motifs, and sequence entanglements.PLoS computational biology · 2023Article
- Characterization and catalytic investigation of fungal single-module nonribosomal peptide synthetase in terpene-amino acid meroterpenoid biosynthesis.Journal of industrial microbiology & biotechnology · 2023Article
- Dynamics and mechanistic interpretations of nonribosomal peptide synthetase cyclization domains.Current opinion in chemical biology · 2023Review
- Biosynthesis of Lyngbyastatins 1 and 3, Cytotoxic Depsipeptides from anJournal of natural products · 2023Article
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Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots of a condensation domain in complex with an aminoacyl-PCP acceptor substrate. These structures allow the identification of a mechanism that controls access of acceptor substrates to the active site in condensation domains. The structures of this complex also allow us to demonstrate that condensation domain active sites do not contain a distinct pocket to select the side chain of the acceptor substrate during peptide assembly but that residues within the active site motif can instead serve to tune the selectivity of these central biosynthetic domains.
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