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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.

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

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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