ArticleNature2008
Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.
Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
66 citing papers in PubMed, 131 citations in OpenAlex.
- Dissecting the role ofFrontiers in microbiology · 2026Article
- Integrated Biofilm Modification and Transcriptional Analysis for Improving Fengycin Production in Bacillus amyloliquefaciens.Probiotics and antimicrobial proteins · 2025Article
- Review on Current Research on Biosynthesis of Biosurfactants and the Regulation Influenced by Metal Ions.Journal of microbiology and biotechnology · 2025Review
- Coniontins, lipopetaibiotics active against Candida auris identified from a microbial natural product fractionation library.Nature communications · 2025Article
- A rational multi-target combination strategy for synergistic improvement of non-ribosomal peptide production.Nature communications · 2025Article
- In-Situ Purification of Non-Ribosomal Peptide Synthetases Assembly Line for Structural and Biochemical Studies.International journal of molecular sciences · 2025Article
- Optimisation of surfactin yield inComputational and structural biotechnology journal · 2024Article
- Research advances in the identification of regulatory mechanisms of surfactin production by Bacillus: a review.Microbial cell factories · 2024Review
- Efficient determination of the accessible conformation space of multi-domain complexes based on EPR PELDOR data.Journal of biomolecular NMR · 2023Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Biosynthetic incorporation of fluorinated amino acids into the nonribosomal peptide gramicidin S.RSC chemical biology · 2023Article
- Protein-protein interface analysis of the non-ribosomal peptide synthetase peptidyl carrier protein and enzymatic domains.Synthetic and systems biotechnology · 2022Review
- Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022Article
- Anti-Mycoplasma Activity of Bacilotetrins C-E, Cyclic Lipodepsipeptides from the Marine-DerivedMarine drugs · 2021Article
- Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations.Protein science : a publication of the Protein Society · 2020Review
- Actinomycete-Derived Polyketides as a Source of Antibiotics and Lead Structures for the Development of New Antimicrobial Drugs.Antibiotics (Basel, Switzerland) · 2019Review
- Genomics-driven discovery of a biosynthetic gene cluster required for the synthesis of BII-Rafflesfungin from the fungus Phoma sp. F3723.BMC genomics · 2019Article
- YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria.The Journal of biological chemistry · 2018Article
- Characterization and heterologous expression of the neoabyssomicin/abyssomicin biosynthetic gene cluster from Streptomyces koyangensis SCSIO 5802.Microbial cell factories · 2018Article
- Structural insights into GDP-mediated regulation of a bacterial acyl-CoA thioesterase.The Journal of biological chemistry · 2017Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) found in bacteria, fungi and plants use two different types of thioesterases for the production of highly active biological compounds. Type I thioesterases (TEI) catalyse the release step from the assembly line of the final product where it is transported from one reaction centre to the next as a thioester linked to a 4'-phosphopantetheine (4'-PP) cofactor that is covalently attached to thiolation (T) domains. The second enzyme involved in the synthesis of these secondary metabolites, the type II thioesterase (TEII), is a crucial repair enzyme for the regeneration of functional 4'-PP cofactors of holo-T domains of NRPS and PKS systems. Mispriming of 4'-PP cofactors by acetyl- and short-chain acyl-residues interrupts the biosynthetic system. This repair reaction is very important, because roughly 80% of CoA, the precursor of the 4'-PP cofactor, is acetylated in bacteria. Here we report the three-dimensional structure of a type II thioesterase from Bacillus subtilis free and in complex with a T domain. Comparison with structures of TEI enzymes shows the basis for substrate selectivity and the different modes of interaction of TEII and TEI enzymes with T domains. Furthermore, we show that the TEII enzyme exists in several conformations of which only one is selected on interaction with its native substrate, a modified holo-T domain.
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What OpenQuestion holds
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.