2bng
STRUCTURE OF AN M.TUBERCULOSIS LEH-LIKE EPOXIDE HYDROLASE
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OverviewOverview
Epoxide hydrolases are vital to many organisms by virtue of their roles in, detoxification, metabolism and processing of signaling molecules. The, Mycobacterium tuberculosis genome encodes an unusually large number of, epoxide hydrolases, suggesting that they might be of particular importance, to these bacteria. We report here the first structure of an epoxide, hydrolase from M.tuberculosis, solved to a resolution of 2.5 A using, single-wavelength anomalous dispersion (SAD) from a, selenomethionine-substituted protein. The enzyme features a deep, active-site pocket created by the packing of three helices onto a curved, six-stranded beta-sheet. This structure is similar to a previously, described limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis and, unlike the alpha/beta-hydrolase fold typical of mammalian epoxide, hydrolases (EH). A number of changes in the mycobacterial enzyme create a, wider and deeper substrate-binding pocket than is found in its Rhodococcus, homologue. Interestingly, each structure contains a different type of, endogenous ligand of unknown origin bound in its active site. As a, consequence of its wider substrate-binding pocket, the mycobacterial EH is, capable of hydrolyzing long or bulky lipophilic epoxides such as, 10,11-epoxystearic acid and cholesterol 5,6-oxide at appreciable rates, suggesting that similar compound(s) will serve as its physiological, substrate(s).
About this StructureAbout this Structure
2BNG is a Single protein structure of sequence from Mycobacterium tuberculosis with CA as ligand. Active as Limonene-1,2-epoxide hydrolase, with EC number 3.3.2.8 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structure of an atypical epoxide hydrolase from Mycobacterium tuberculosis gives insights into its function., Johansson P, Unge T, Cronin A, Arand M, Bergfors T, Jones TA, Mowbray SL, J Mol Biol. 2005 Sep 2;351(5):1048-56. PMID:16051262
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