ArticleActa crystallographica. Section F, Structural biology communications2022
Crystal structure determination of the halogenase CtcP from Streptomyces aureofaciens.
Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 3 citations in OpenAlex.
- Structural Basis of Regioselective Bromination of Tricyclic Tryptoline by the Tryptophan Halogenase Thal.Chembiochem : a European journal of chemical biology · 2025Article
- Crystal structures and low-affinity complex formation of halogenase CtcP and FAD reductase CtcQ from the chlortetracycline biosynthetic pathway.Bioscience reports · 2025Article
- Site-selective chlorination of pyrrolic heterocycles by flavin dependent enzyme PrnC.Communications chemistry · 2024Article
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1 author at 1 institution in 1 country.
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Abstract
Chlortetracycline (CTC), a derivative of tetracycline (TC), is a broadly used antibiotic that inhibits the synthesis of bacterial proteins by competing with the A-site tRNA on ribosomes. A recent study showed that during the biosynthesis of CTC in Streptomyces aureofaciens, the halogenase CtcP catalyzes the final chlorination reaction and transforms TC into CTC. However, the structure of this fundamental enzyme is still lacking. Here, selenomethionine-derivatized CtcP from S. aureofaciens was overexpressed and purified and its structure was determined at 2.7 Å resolution. The structure of CtcP reveals the conserved monooxygenase domain shared by all flavin-dependent halogenases and a unique C-terminal domain. Although FAD was not observed in the structure, the monooxygenase domain has a conserved FAD-binding pocket and active center. The C-terminal domain displays an α-helical bundle fold, which could contribute to substrate specificity. This work provides a molecular basis for enzyme engineering to improve the industrial production of CTC.
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