2vf2
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X-RAY CRYSTAL STRUCTURE OF HSAD FROM MYCOBACTERIUM TUBERCULOSIS
OverviewOverview
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.
About this StructureAbout this Structure
2VF2 is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Active as 2,6-dioxo-6-phenylhexa-3-enoate hydrolase, with EC number 3.7.1.8 Known structural/functional Sites: , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosis., Lack N, Lowe ED, Liu J, Eltis LD, Noble ME, Sim E, Westwood IM, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):2-7., Epub 2007 Dec 20. PMID:18097091
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