ArticleACS chemical biology2014
A distinct MaoC-like enoyl-CoA hydratase architecture mediates cholesterol catabolism in Mycobacterium tuberculosis.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 67 citations in OpenAlex.
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- Uncovering resistance pathways to first- and last-line antibiotics inMicrobial genomics · 2026Article
- Identification of the C9-hydrogenase for 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid (9,17-DOHNA) and the 7α-dehydratase essential for initiating β-oxidation of the B-, C-, and D-rings in steroid degradation byApplied and environmental microbiology · 2026Article
- Identification of dehydrogenase, hydratase, and aldolase responsible for the propionyl residue removal in degradation of cholic acid C-17 side chain inMicrobiology spectrum · 2025Article
- Efficient Synthesis of Steroidal Intermediates with a C17 Side Chain from Phytosterols by Genetically Modified Mycolicibacterium neoaurum NRRL B-3805 Strain.ChemistryOpen · 2025Article
- Comprehensive Bioinformatics Analysis for the Identification of Hub Genes and Critical Signaling Pathways Differentiating Latent and Active Tuberculosis.Combinatorial chemistry & high throughput screening · 2025Article
- Analysis of the Diversity and Functional Potential of Bacterial Communities in Tuberculomas.Bulletin of experimental biology and medicine · 2024Article
- Article
- HadBD dehydratase from Mycobacterium tuberculosis fatty acid synthase type II: A singular structure for a unique function.Protein science : a publication of the Protein Society · 2024Article
- Unravelling and engineering an operon involved in the side-chain degradation of sterols in Mycolicibacterium neoaurum for the production of steroid synthons.Biotechnology for biofuels and bioproducts · 2023Article
- Crystal Structure of Mesaconyl-CoA Hydratase fromJournal of microbiology and biotechnology · 2023Article
- Targeted Mutagenesis of Mycobacterium Strains by Homologous Recombination.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Bioconversion of Phytosterols to 9-Hydroxy-3-Oxo-4,17-Pregadiene-20-Carboxylic Acid Methyl Ester by Enoyl-CoA Deficiency and Modifying Multiple Genes in Mycolicibacterium neoaurum.Applied and environmental microbiology · 2022Article
- Bacterial Hydratases Involved in Steroid Side Chain Degradation Have Distinct Substrate Specificities.Journal of bacteriology · 2022Article
- Multiple acyl-CoA dehydrogenase deficiency kills Mycobacterium tuberculosis in vitro and during infection.Nature communications · 2021Article
- Comparative Analysis of Bile-Salt Degradation inApplied and environmental microbiology · 2021Article
- Proteome, Bioinformatic, and Functional Analyses Reveal a Distinct and Conserved Metabolic Pathway for Bile Salt Degradation in theApplied and environmental microbiology · 2021Article
- Degradation of Bile Acids by Soil and Water Bacteria.Microorganisms · 2021Review
- Enzymatic β-Oxidation of the Cholesterol Side Chain inACS infectious diseases · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Mycobacterium tuberculosis (Mtb) igr operon plays an essential role in Mtb cholesterol metabolism, which is critical for pathogenesis during the latent stage of Mtb infection. Here we report the first structure of a heterotetrameric MaoC-like enoyl-CoA hydratase, ChsH1-ChsH2, which is encoded by two adjacent genes from the igr operon. We demonstrate that ChsH1-ChsH2 catalyzes the hydration of a steroid enoyl-CoA, 3-oxo-4,17-pregnadiene-20-carboxyl-CoA, in the modified β-oxidation pathway for cholesterol side chain degradation. The ligand-bound and apoenzyme structures of ChsH1-ChsH2(N) reveal an unusual, modified hot-dog fold with a severely truncated central α-helix that creates an expanded binding site to accommodate the bulkier steroid ring system. The structures show quaternary structure shifts that accommodate the four rings of the steroid substrate and offer an explanation for why the unusual heterotetrameric assembly is utilized for hydration of this steroid. The unique αβ heterodimer architecture utilized by ChsH1-ChsH2 to bind its distinctive substrate highlights an opportunity for the development of new antimycobacterial drugs that target a pathway specific to Mtb.
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