2bng

File:2bng.gif

spinqualitylabelsall models 2bng, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [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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