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

    Browse

    All of KAUSTCommunitiesIssue DateSubmit DateThis CollectionIssue DateSubmit Date

    My Account

    Login

    Quick Links

    Open Access PolicyORCID LibguideTheses and Dissertations LibguideSubmit an Item

    Statistics

    Display statistics

    Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    acschembio.7b00792.pdf
    Size:
    1.539Mb
    Format:
    PDF
    Description:
    Accepted Manuscript
    Download
    Type
    Article
    Authors
    Grötzinger, Stefan W.
    Karan, Ram
    Strillinger, Eva cc
    Bader, Stefan
    Frank, Annika
    Al Rowaihi, Israa cc
    Gespers (Akal), Anastassja cc
    Wackerow, Wiebke
    Archer, John A.C. cc
    Rueping, Magnus cc
    Weuster-Botz, Dirk
    Groll, Michael
    Eppinger, Jörg cc
    Arold, Stefan T. cc
    KAUST Department
    Biological & Organometallic Catalysis Laboratories
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Chemical Science Program
    Computational Bioscience Research Center (CBRC)
    KAUST Catalysis Center (KCC)
    Office of the VP
    Physical Science and Engineering (PSE) Division
    Structural Biology and Engineering
    KAUST Grant Number
    URF/1/1976.06
    URF/1/2602.01.01
    URF/1/1974
    Date
    2017-12-18
    Online Publication Date
    2017-12-18
    Print Publication Date
    2018-01-19
    Permanent link to this record
    http://hdl.handle.net/10754/626319
    
    Metadata
    Show full item record
    Abstract
    Because only 0.01% of prokaryotic genospecies can be cultured and in situ observations are often impracticable, culture-independent methods are required to understand microbial life and harness potential applications of microbes. Here, we report a methodology for the production of proteins with desired functions based on single amplified genomes (SAGs) from unculturable species. We use this method to resurrect an alcohol dehydrogenase (ADH/D1) from an uncharacterized halo-thermophilic archaeon collected from a brine pool at the bottom of the Red Sea. Our crystal structure of 5,6-dihydroxy NADPH-bound ADH/D1 combined with biochemical analyses reveal the molecular features of its halo-thermophily, its unique habitat adaptations, and its possible reaction mechanism for atypical oxygen activation. Our strategy offers a general guide for using SAGs as a source for scientific and industrial investigations of ‘microbial dark matter’.
    Citation
    Grötzinger SW, Karan R, Strillinger E, Bader S, Frank A, et al. (2017) Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes. ACS Chemical Biology. Available: http://dx.doi.org/10.1021/acschembio.7b00792.
    Sponsors
    The research reported in this publication was supported by the King Abdullah University of Science and Technology (KAUST) through the baseline fund and the Office of Sponsored Research (OSR) under award nos. URF/1/1976.06, URF/1/2602.01.01, and URF/1/1974. The authors are thankful for support for E.S. and S.G. from the International Graduate School of Science and Engineering (IGGSE), Technical University of Munich (TUM), project 8.03.
    Publisher
    American Chemical Society (ACS)
    Journal
    ACS Chemical Biology
    DOI
    10.1021/acschembio.7b00792
    Additional Links
    http://pubs.acs.org/doi/abs/10.1021/acschembio.7b00792
    ae974a485f413a2113503eed53cd6c53
    10.1021/acschembio.7b00792
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program; Physical Science and Engineering (PSE) Division; Chemical Science Program; KAUST Catalysis Center (KCC); Computational Bioscience Research Center (CBRC)

    entitlement

     
    DSpace software copyright © 2002-2022  DuraSpace
    Quick Guide | Contact Us | KAUST University Library
    Open Repository is a service hosted 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. For anonymous users the allowed maximum amount is 50 search results.

    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.