ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Degradation of CCurrent microbiology · 2025Article
- Ring A Cleaving Beta-Diketone Hydrolase Is a Key Enzyme of Steroid Degradation in Anaerobic Bacteria.Environmental microbiology · 2025Article
- Degradation of Bile Acids by Soil and Water Bacteria.Microorganisms · 2021Review
- Review
- Investigation of the mycobacterial enzyme HsaD as a potential novel target for anti-tubercular agents using a fragment-based drug design approach.British journal of pharmacology · 2017Article
- Cholesterol metabolism: a potential therapeutic target in Mycobacteria.British journal of pharmacology · 2017Review
- Lipidomics Characterization of Biosynthetic and Remodeling Pathways of Cardiolipins in Genetically and Nutritionally Manipulated Yeast Cells.ACS chemical biology · 2017Article
- Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site.Scientific reports · 2016Article
- Production of recombinant proteins in Mycobacterium smegmatis for structural and functional studies.Protein science : a publication of the Protein Society · 2015Review
- The lid domain of the MCP hydrolase DxnB2 contributes to the reactivity toward recalcitrant PCB metabolites.Biochemistry · 2013Article
- Updating and curating metabolic pathways of TB.Tuberculosis (Edinburgh, Scotland) · 2013Review
- Catabolism and biotechnological applications of cholesterol degrading bacteria.Microbial biotechnology · 2012Review
- Cholesterol catabolism as a therapeutic target in Mycobacterium tuberculosis.Trends in microbiology · 2011Review
- Characterization of a carbon-carbon hydrolase from Mycobacterium tuberculosis involved in cholesterol metabolism.The Journal of biological chemistry · 2010Article
- Identification of arylamine N-acetyltransferase inhibitors as an approach towards novel anti-tuberculars.Protein & cell · 2010Article
- Arylamine N-acetyltransferases in mycobacteria.Current drug metabolism · 2008Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Tuberculosis is a major cause of death worldwide. Understanding of the pathogenicity of Mycobacterium tuberculosis has been advanced by gene analysis and has led to the identification of genes that are important for intracellular survival in macrophages. One of these genes encodes HsaD, a meta-cleavage product (MCP) hydrolase that catalyzes the hydrolytic cleavage of a carbon-carbon bond in cholesterol metabolism. This paper describes the production of HsaD as a recombinant protein and, following crystallization, the determination of its three-dimensional structure to 2.35 A resolution by X-ray crystallography at the Diamond Light Source in Oxfordshire, England. To the authors' knowledge, this study constitutes the first report of a structure determined at the new synchrotron facility. The volume of the active-site cleft of the HsaD enzyme is more than double the corresponding active-site volumes of related MCP hydrolases involved in the catabolism of aromatic compounds, consistent with the specificity of HsaD for steroids such as cholesterol. Knowledge of the structure of the enzyme facilitates the design of inhibitors.
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