2bng
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STRUCTURE OF AN M.TUBERCULOSIS LEH-LIKE EPOXIDE HYDROLASE
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 ... [(full description)]
About this StructureAbout this Structure
2BNG is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with CA as [ligand]. Active as [[1]], with EC number [3.3.2.8]. 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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