Opendata, web and dolomites

FLUOROKEF

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

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 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.

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

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

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "FLUOROKEF" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "FLUOROKEF" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.3.2.)

NSTree (2020)

Understanding substrate delivery for cell wall biosynthesis in plants

Read More  

EngPTC2 (2019)

Exploring new technologies for the next generation pulse tube cryocooler below 2K

Read More  

MemoryAggregates (2020)

Mechanism of Whi3 Aggregation and its Age-dependent Malfunction

Read More