5uro

Structure of a soluble epoxide hydrolase identified in Trichoderma reesei

spinqualitylabelsall models 5uro, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5uro is a 1 chain structure with sequence from Trichoderma reesei QM6a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.701Å Ligands: 8LD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0R7E2_HYPJQ Publication Abstract from PubMed Epoxide hydrolases (EHs) are enzymes that have high biotechnological interest for the fine and transformation industry. Several of these enzymes have enantioselectivity, which allows their application in the separation of enantiomeric mixtures of epoxide substrates. Although two different families of EHs have been described, those that have the alpha/beta-hidrolase fold are the most explored for biotechnological purpose. These enzymes are functionally very well studied, but only few members have three-dimensional structures characterised. Recently, a new EH from the filamentous fungi Trichoderma reseei (TrEH) has been discovered and functionally studied. This enzyme does not have high homology to any other EH structure and have an enatiopreference for (S)-(-) isomers. Herein we described the crystallographic structure of TrEH at 1.7A resolution, which reveals features of its tertiary structure and active site. TrEH has a similar fold to the other soluble epoxide hydrolases and has the two characteristic hydrolase and cap domains. The enzyme is predominantly monomeric in solution and has also been crystallised as a monomer in the asymmetric unit. Although the catalytic residues are conserved, several other residues of the catalytic groove are not, and might be involved in the specificity for substrates and in the enantioselectivy of this enzyme. In addition, the determination of the crystallographic structure of TrEH might contribute to the rational site direct mutagenesis to generate an even more stable enzyme with higher efficiency to be used in biotechnological purposes. Structure of a soluble epoxide hydrolase identified in Trichoderma reesei.,Wilson C, De Oliveira GS, Adriani PP, Chambergo FS, Dias MVB Biochim Biophys Acta. 2017 Aug;1865(8):1039-1045. doi:, 10.1016/j.bbapap.2017.05.004. Epub 2017 May 11. PMID:28502798 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exportin 3D structures

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