ArticleActa crystallographica. Section D, Structural biology2019
Crystal structure of Mycobacterium tuberculosis FadB2 implicated in mycobacterial β-oxidation.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Essential redundancies fuel Mycobacterium tuberculosis adaptation to the host.PLoS pathogens · 2025Review
- Defining the mechanism of action of the nitrofuranyl piperazine HC2210 against Mycobacterium abscessus.npj antimicrobials and resistance · 2025Article
- Differential expression of genes associated with lipid import, β-oxidation and lactate oxidation induced byJournal of medical microbiology · 2025Article
- TopEnzyme: a framework and database for structural coverage of the functional enzyme space.Bioinformatics (Oxford, England) · 2023Article
- The mutation rate of rpoB gene showed an upward trend with the increase of MIRU10, MIRU39 and QUB4156 repetitive number.BMC genomics · 2023Article
- Salinomycin biosynthesis reversely regulates the β-oxidation pathway in Streptomyces albus by carrying a 3-hydroxyacyl-CoA dehydrogenase gene in its biosynthetic gene cluster.Microbial biotechnology · 2022Article
- Comparative Analysis on Proteomics Profiles of Intracellular and ExtracellularFrontiers in genetics · 2022Article
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6 authors.
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Abstract
The intracellular pathogen Mycobacterium tuberculosis is the causative agent of tuberculosis, which is a leading cause of mortality worldwide. The survival of M. tuberculosis in host macrophages through long-lasting periods of persistence depends, in part, on breaking down host cell lipids as a carbon source. The critical role of fatty-acid catabolism in this organism is underscored by the extensive redundancy of the genes implicated in β-oxidation (∼100 genes). In a previous study, the enzymology of the M. tuberculosis L-3-hydroxyacyl-CoA dehydrogenase FadB2 was characterized. Here, the crystal structure of this enzyme in a ligand-free form is reported at 2.1 Å resolution. FadB2 crystallized as a dimer with three unique dimer copies per asymmetric unit. The structure of the monomer reveals a dual Rossmann-fold motif in the N-terminal domain, while the helical C-terminal domain mediates dimer formation. Comparison with the CoA- and NAD
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