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dc.contributor.authorHarb, L.
dc.contributor.authorArooj, Mahreen
dc.contributor.authorVrielink, A.
dc.contributor.authorMancera, Ricardo
dc.identifier.citationHarb, L. and Arooj, M. and Vrielink, A. and Mancera, R. 2017. Computational site-directed mutagenesis studies of the role of the hydrophobic triad on substrate binding in cholesterol oxidase. Proteins: Function, Structure, and Bioinformatics. 85 (9): pp. 1645-1655.

© 2017 Wiley Periodicals, Inc. Cholesterol oxidase (ChOx) is a flavoenzyme that oxidizes and isomerizes cholesterol (CHL) to form cholest-4-en-3-one. Molecular docking and molecular dynamics simulations were conducted to predict the binding interactions of CHL in the active site. Several key interactions (E361-CHL, N485-FAD, and H447-CHL) were identified and which are likely to determine the correct positioning of CHL relative to flavin-adenine dinucleotide (FAD). Binding of CHL also induced changes in key residues of the active site leading to the closure of the oxygen channel. A group of residues, Y107, F444, and Y446, known as the hydrophobic triad, are believed to affect the binding of CHL in the active site. Computational site-directed mutagenesis of these residues revealed that their mutation affects the conformations of key residues in the active site, leading to non-optimal binding of CHL and to changes in the structure of the oxygen channel, all of which are likely to reduce the catalytic efficiency of ChOx. Proteins 2017; 85:1645–1655. © 2017 Wiley Periodicals, Inc.

dc.publisherJohn Wiley & Sons, Inc.
dc.titleComputational site-directed mutagenesis studies of the role of the hydrophobic triad on substrate binding in cholesterol oxidase
dc.typeJournal Article
dcterms.source.titleProteins: Function, Structure, and Bioinformatics
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available

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