5URO

Structure of a soluble epoxide hydrolase identified in Trichoderma reesei

Summary for 5URO

• Entry DOI: 10.2210/pdb5uro/pdb
• Descriptor: Predicted protein, 2,2'-oxydi(ethyn-1-ol) (3 entities in total)
• Functional Keywords: epoxide hydrolase; trichoderma reesei, hydrolase
• Biological source: Hypocrea jecorina (strain QM6a)
• Total number of polymer chains: 1
• Total formula weight: 37632.74

Authors

Wilson, C.,de Oliveira, G.,Chambergo, F.,Dias, M.V.B. (deposition date: 2017-02-11, release date: 2017-05-31, Last modification date: 2023-10-04)

Primary citation

Wilson, C.,De Oliveira, G.S.,Adriani, P.P.,Chambergo, F.S.,Dias, M.V.B.
Structure of a soluble epoxide hydrolase identified in Trichoderma reesei.
Biochim. Biophys. Acta, 1865:1039-1045, 2017

PubMed Abstract: 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 α/β-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 1.7Å 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.

PubMed: 28502798
DOI: 10.1016/j.bbapap.2017.05.004

Experimental method

X-RAY DIFFRACTION (1.701 Å)