1nu3
From Proteopedia
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Limonene-1,2-epoxide hydrolase in complex with valpromide
Overview
Epoxide hydrolases are essential for the processing of epoxide-containing, compounds in detoxification or metabolism. The classic epoxide hydrolases, have an alpha/beta hydrolase fold and act via a two-step reaction, mechanism including an enzyme-substrate intermediate. We report here the, structure of the limonene-1,2-epoxide hydrolase from Rhodococcus, erythropolis, solved using single-wavelength anomalous dispersion from a, selenomethionine-substituted protein and refined at 1.2 A resolution. This, enzyme represents a completely different structure and a novel one-step, mechanism. The fold features a highly curved six-stranded mixed, beta-sheet, with four alpha-helices packed onto it to create a deep, pocket. Although most residues lining this pocket are hydrophobic, a, cluster of polar groups, including an Asp-Arg-Asp triad, interact at its, deepest point. Site-directed mutagenesis supports the conclusion that this, is the active site. Further, a 1.7 A resolution structure shows the, inhibitor valpromide bound at this position, with its polar atoms, interacting directly with the residues of the triad. We suggest that, several bacterial proteins of currently unknown function will share this, structure and, in some cases, catalytic properties.
About this Structure
1NU3 is a Single protein structure of sequence from Rhodococcus erythropolis with MES and VPR as ligands. Active as Limonene-1,2-epoxide hydrolase, with EC number 3.3.2.8 Full crystallographic information is available from OCA.
Reference
Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site., Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, de Bont JA, Jones TA, Mowbray SL, EMBO J. 2003 Jun 2;22(11):2583-92. PMID:12773375
Page seeded by OCA on Tue Nov 20 22:33:37 2007
