ArticleActa crystallographica. Section D, Structural biology2023
Structural basis of the amidase ClbL central to the biosynthesis of the genotoxin colibactin.
Article in Acta crystallographica. Section D, Structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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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.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Advances in amidases and urethanases as depolymerization biocatalysts.Nature chemical biology · 2026Review
- The human microbiome as a source of novel bioactive natural products: structures, bioactivities, and biosynthetic insights.Journal of natural medicines · 2026Review
- A Modular Biosensor Platform for the Detection of Plastic Monomers and the Engineering of Promiscuous Amidases Toward Challenging Substrates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Insights into the Catalytic Activity of a Metagenome-Derived Urethanase.Journal of the American Chemical Society · 2025Article
- Structure-Guided Engineering of a Versatile Urethanase Improves Its Polyurethane Depolymerization Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Colibactin is a genotoxic natural product produced by select commensal bacteria in the human gut microbiota. The compound is a bis-electrophile that is predicted to form interstrand DNA cross-links in target cells, leading to double-strand DNA breaks. The biosynthesis of colibactin is carried out by a mixed NRPS-PKS assembly line with several noncanonical features. An amidase, ClbL, plays a key role in the pathway, catalyzing the final step in the formation of the pseudodimeric scaffold. ClbL couples α-aminoketone and β-ketothioester intermediates attached to separate carrier domains on the NRPS-PKS assembly. Here, the 1.9 Å resolution structure of ClbL is reported, providing a structural basis for this key step in the colibactin biosynthetic pathway. The structure reveals an open hydrophobic active site surrounded by flexible loops, and comparison with homologous amidases supports its unusual function and predicts macromolecular interactions with pathway carrier-protein substrates. Modeling protein-protein interactions supports a predicted molecular basis for enzyme-carrier domain interactions. Overall, the work provides structural insight into this unique enzyme that is central to the biosynthesis of colibactin.
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Registered trials
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