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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.

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

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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