• Login
    View Item 
    •   Home
    • Department of Drug design and optimization ([HIPS]DDOP)
    • publications of the research group drug design and optimization(HIPS]DDOP)
    • View Item
    •   Home
    • Department of Drug design and optimization ([HIPS]DDOP)
    • publications of the research group drug design and optimization(HIPS]DDOP)
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of HZICommunitiesTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)This CollectionTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)

    My Account

    LoginRegister

    Local Links

    About: PolicyHelmholtz-Zentrum für Infektionsforschung HomepageHZI-Library HomepageContact usOpen AccessPublishing ApproachGetting StartedEditing ProfileBrowsing OptionsUsing SearchSubmitting ContentLicenced Journals & access details here

    Statistics

    Display statistics

    Molecular basis of HHQ biosynthesis: molecular dynamics simulations, enzyme kinetic and surface plasmon resonance studies

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    13628_2012_Article_53.pdf
    Size:
    1.032Mb
    Format:
    PDF
    Download
    Average rating
     
       votes
    Cast your vote
    You can rate an item by clicking the amount of stars they wish to award to this item. When enough users have cast their vote on this item, the average rating will also be shown.
    Star rating
     
    Your vote was cast
    Thank you for your feedback
    Authors
    Steinbach, Anke
    Maurer, Christine K
    Weidel, Elisabeth
    Henn, Claudia
    Brengel, Christian
    Hartmann, Rolf W
    Negri, Matthias
    Issue Date
    2013-08-01
    
    Metadata
    Show full item record
    Abstract
    Abstract Background PQS (P seudomonas Quinolone Signal) and its precursor HHQ are signal molecules of the P. aeruginosa quorum sensing system. They explicate their role in mammalian pathogenicity by binding to the receptor PqsR that induces virulence factor production and biofilm formation. The enzyme PqsD catalyses the biosynthesis of HHQ. Results Enzyme kinetic analysis and surface plasmon resonance (SPR) biosensor experiments were used to determine mechanism and substrate order of the biosynthesis. Comparative analysis led to the identification of domains involved in functionality of PqsD. A kinetic cycle was set up and molecular dynamics (MD) simulations were used to study the molecular bases of the kinetics of PqsD. Trajectory analysis, pocket volume measurements, binding energy estimations and decompositions ensured insights into the binding mode of the substrates anthraniloyl-CoA and β-ketodecanoic acid. Conclusions Enzyme kinetics and SPR experiments hint at a ping-pong mechanism for PqsD with ACoA as first substrate. Trajectory analysis of different PqsD complexes evidenced ligand-dependent induced-fit motions affecting the modified ACoA funnel access to the exposure of a secondary channel. A tunnel-network is formed in which Ser317 plays an important role by binding to both substrates. Mutagenesis experiments resulting in the inactive S317F mutant confirmed the importance of this residue. Two binding modes for β-ketodecanoic acid were identified with distinct catalytic mechanism preferences.
    Citation
    BMC Biophysics. 2013 Aug 01;6(1):10
    URI
    http://dx.doi.org/10.1186/2046-1682-6-10
    http://hdl.handle.net/10033/620948
    Type
    Journal Article
    Collections
    publications of the research group drug design and optimization(HIPS]DDOP)

    entitlement

     

    DSpace software copyright © 2002-2023  DuraSpace
    Quick Guide | Kontakt | Feedback abschicken
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.