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ACPNMR

Structural dynamics of acyl carrier protein complexes through combined solution and solid-state NMR

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 ACPNMR project word cloud

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

toolbox    magnitude    specificity    vital    relaxation    acp12a    solid    dynamics    nature    antibiotics    carrier    probe    adapter    synthesize    synthase    size    chemical    drugs    biosythesized    combining    direct    dynamical    good    protein    picture    interactions    molecular    genetic    structure    successful    inactive    crisis    arsenal    assembly    polyketide    neglecting    modifying    paving    inspired    ing    obtain    directionality    responsible    module    pkss    pks    bacterium    becomes    complexes    orders    isolated    industrial    manipulation    ketosynthase    lines    understand    infected    active    compounds    resistant    ks12    special    nmr    proteins    resistance    gladiolinum    acp12b    modular    solution    multienzymatic    12    motions    microorganisms    mulitenzyme    synthetic    world    ideal    medicine    mycobacterium    gladiolin    shown    biology    producing    multidrug    dysfunctional    natural    biosynthesis    difficult    acyl    acps    population    structural    tuberculosis    dynamic    modern   

Project "ACPNMR" data sheet

The following table provides information about the project.

Coordinator
THE UNIVERSITY OF WARWICK 

Organization address
address: Kirby Corner Road - University House
city: COVENTRY
postcode: CV4 8UW
website: www.warwick.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]
 Project website https://www.facebook.com/drpotocki.msc
 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 2015-09-10   to  2017-09-09

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE UNIVERSITY OF WARWICK UK (COVENTRY) coordinator 183˙454.00

Map

 Project objective

'Antibiotics are a vital part of modern medicine. However, the available arsenal of antibiotics becomes less effective as microorganisms develop 'resistance' against them. The resulting crisis in medicine necessitates development of new drugs. Natural products inspired compounds are a potential solution to this challenge. For example, gladiolin biosythesized by a mulitenzyme polyketide synthase (PKS) was shown to be active against Mycobacterium tuberculosis, a multidrug resistant bacterium that one third of world’s population is infected with. The PKS producing gladiolinum is a good example of multienzymatic assembly lines that due to their modular nature are ideal for genetic manipulation paving the way for synthetic biology approach to produce new drugs (that are difficult to synthesize using chemical methods). However, for such approach to be successful it is crucial to understand molecular level structural and dynamical factors responsible for controlling directionality and specificity of biosynthesis. Neglecting such factors, when modifying PKSs often results in assembly lines that are inactive or dysfunctional. Here we propose to use a novel approach combining state-of-the-art solution and solid-state NMR methods to investigate structure, dynamics and interactions of proteins from module 12 of gladiolin PKS, particularly acyl carrier proteins (ACP12a and ACP12b) and special adapter ketosynthase (KS12), all of them highly required in industrial biosynthesis toolbox. We will use solution NMR to characterize isolated ACPs and solid-state NMR to study ACPs-KS12 complexes (direct structural information is difficult to obtain by solution NMR due to the large complex size). Combining solution and solid-state NMR relaxation methods will allow us to probe protein motions over 6 orders of magnitude providing a comprehensive picture of relevant dynamic changes in ACPs-KS12 complexes.'

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

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