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FLUOROKEF

Incorporation of unnatural fluorinated amino acids to probe the function of the bacterial efflux system Kef in a cellular setting.

Total Cost €

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EC-Contrib. €

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Partnership

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 FLUOROKEF project word cloud

Explore the words cloud of the FLUOROKEF project. It provides you a very rough idea of what is the project "FLUOROKEF" about.

escherichia    441    full    eckefctd    ray    trifluromethyl    shewanella    f448tfmf    employed    construct    lack    vitro    vital    potassium    dynamics    bacteria    stop    bauer    ligands    crystallographic    denitrificans    gain    sdkef    molecular    function    disc    quantitatively    electrophilic    mechanism    19f    conformation    hypothesis    wish    phenylalanine    allowed    employ    monitor    kd    cytoplasm    soluble    inhibitors    activation    f448    nmr    length    conserved    efflux    kirby    dynamic    physiologically    tfmf    compounds    affinities    activators    terminal    cellular    protects    cell    amber    homeostasis    sdkefctd    detrimental    coli    generation    acidification    direct    antibiotic    probe    truncated    diffusion    assays    kill    replace    understand    indicates    cells    data    f441    biophysical    inside    drugs    channel    library    codon    maintaining    screen    residue    transformants    domain    binding    kef    extend    antibiotics   

Project "FLUOROKEF" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD 

Organization address
address: WELLINGTON SQUARE UNIVERSITY OFFICES
city: OXFORD
postcode: OX1 2JD
website: www.ox.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 183˙454 €
 EC max contribution 183˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2015
 Duration (year-month-day) from 2015-10-01   to  2017-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD UK (OXFORD) coordinator 183˙454.00

Map

 Project objective

The potassium efflux system, Kef, protects bacteria against the detrimental effects of electrophilic compounds via acidification of the cytoplasm. Its vital role in maintaining cell homeostasis makes Kef a promising target for antibiotics, but such drugs can be developed only with a molecular understanding of Kef activation. Our work indicates that phenylalanine residue 441 (F441) in Escherichia coli is crucial for the activation of K efflux. This mechanism is conserved, and F448 of Shewanella denitrificans Kef (SdKef) has the same function. This work employed X-ray crystallographic studies using a truncated construct of the E. coli Kef soluble C-terminal domain (EcKefCTD) and biophysical studies conducted on the SdKef C-terminal domain (SdKefCTD). While the crystallographic studies have been essential in hypothesis generation, they lack the dynamic aspect that is required to understand the mechanism of Kef activation. Although the use of a truncated construct has allowed development of biophysical assays, we wish to extend our work to focus on the full-length channel. To achieve these aims we will employ whole cell 19F NMR to probe the function of Kef.

To determine if 19F NMR can be used to monitor F448 conformation, we will employ amber stop codon technology to replace F448 of SdKef with 4-trifluromethyl-L-phenylalanine (tfmF). We will monitor the dynamics of F448tfmF by 19F NMR upon binding of activators and inhibitors, using our library of SdKef ligands. To gain an understanding of Kef activation in cells, we will quantitatively determine binding affinities of the Kef ligands to SdKef(F448tfmF), in E. coli transformants using in-cell 19F NMR. This direct determination of binding inside the cells will be more physiologically relevant than the in vitro KD data. To assess the antibiotic activity of compounds that show cellular activity against Kef, we will employ the Kirby-Bauer disc diffusion method to screen for compounds that can kill bacteria.

 Publications

year authors and title journal last update
List of publications.
2017 Christos Pliotas, Samuel C. Grayer, Silvia Ekkerman, Anthony K. N. Chan, Jess Healy, Phedra Marius, Wendy Bartlett, Amjad Khan, Wilian A. Cortopassi, Shane A. Chandler, Tim Rasmussen, Justin L. P. Benesch, Robert S. Paton, Timothy D. W. Claridge, Samantha Miller, Ian R. Booth, James H. Naismith, Stuart J. Conway
Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System
published pages: 4219-4234, ISSN: 0006-2960, DOI: 10.1021/acs.biochem.7b00300
Biochemistry 56/32 2019-06-18

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