Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Computational site-directed mutagenesis studies of the role of the hydrophobic triad on substrate binding in cholesterol oxidase

    Access Status
    Fulltext not available
    Authors
    Harb, L.
    Arooj, Mahreen
    Vrielink, A.
    Mancera, Ricardo
    Date
    2017
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Harb, 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.
    Source Title
    Proteins: Function, Structure, and Bioinformatics
    DOI
    10.1002/prot.25319
    ISSN
    0887-3585
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/63291
    Collection
    • Curtin Research Publications
    Abstract

    © 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.

    Related items

    Showing items related by title, author, creator and subject.

    • Structure/function studies of 5a-reductase.
      Baxter, Fiona O. (2001)
      This thesis reports structure-function assessments made using site-directed mutagenesis of the human enzyme 5alpha-reductase (5AR), an enzyme crucial for normal masculine development. These assessments utilised the ...
    • Molecular modelling of the interactions of complex carbohydrates with proteins
      Gandhi, Neha Sureshchandra (2011)
      Glycosaminoglycans (GAGs) are ubiquitous complex carbohydrate molecules present on the cell surfaces and in extracellular matrices (ECM) of vertebrate and invertebrate tissues. The interactions of sulphated GAGs such as ...
    • Differential Effects of Methoxy Group on the Interaction of Curcuminoids with Two Major Ligand Binding Sites of Human Serum Albumin
      Sato, H.; Chuang, Victor; Yamasaki, K.; Yamaotsu, N.; Watanabe, H.; Nagumo, K.; Anraku, M.; Kadowaki, D.; Ishima, Y.; Hirono, S.; Otagiri, M.; Maruyama, T. (2014)
      Curcuminoids are a group of compounds with a similar chemical backbone structure but containing different numbers of methoxy groups that have therapeutic potential due to their anti-inflammatory and anti-oxidant properties. ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.