Structure of a large non-crystalline multiprotein assembly by solid-state nuclear magnetic resonance with ultra-fast magic-angle spinning

Información del proyecto

COMPLEX-fastMAS-NMR

Identificador del acuerdo de subvención: 661799

DOI

10.3030/661799

Proyecto cerrado

Fecha de la firma de la CE 31 Marzo 2015

Fecha de inicio 1 Enero 2016

Fecha de finalización 18 Enero 2018

Financiado con arreglo a

• EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions

Coste total

€ 185 076,00

Aportación de la UE

€ 185 076,00

Coordinado por

CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS
France

Objetivo

Extrapolating from protein structure to function is an operation difficult to accomplish, as most functions in the cell are not carried out by single proteins, but by macromolecular complexes containing multiple subunits endowed with specific functions. Despite the many advances in structural and biochemical studies of isolated molecules, a comprehensive portrait of cell biochemistry must thus include insights of the supramolecular network of interactions among the individual constituents. The structure determination of large and dynamical protein ensembles presents a great deal of challenges for X-ray diffraction techniques, and for solution nuclear magnetic resonance (NMR) due to the large size of these objects. Consequently, there is little information available today on the overall organization of the assembly subunits, their interactions, and sometimes their precise function within the cell. High-resolution solid-state NMR (ssNMR) has recently developed as a powerful structural tool for studying structure and dynamics of solid biological samples at atomic resolution. A number of issues remain however to be addressed before ssNMR is ready to cope with large-sized multi-domain functional assemblies.
The proposed project aims to capitalize on new concepts recently introduced by the host institution, to implement innovative solid-state NMR methodologies. Sophisticated experimental approaches will be introduced at high magnetic field, in combination with ultra-fast magic angle spinning (MAS), enabling the structure characterization of non-crystalline assemblies that cannot be currently carried out by any other experimental technique, and notably, the determination at atomic level of the structural details that govern protein-protein interactions in functional assemblies. As a benchmark, we will tackle the interaction mode of the ring-shaped hexameric DnaB helicase with its partner DnaC, an assembly that controls the origin of the DNA replication in E. coli.

Ámbito científico (EuroSciVoc)

• ciencias naturales › ciencias biológicas › bioquímica › biomoléculas › proteínas › proteómica
• ciencias naturales › ciencias biológicas › bioquímica › biomoléculas › ácido nucleico
• ciencias naturales › ciencias biológicas › microbiología › bacteriología
• ciencias naturales › ciencias biológicas › genética › ADN
• ciencias naturales › ciencias biológicas › genética › ARN

Programa(s)

• H2020-EU.1.3. - EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions PROGRAMA PRINCIPAL
  
• H2020-EU.1.3.2. - Nurturing excellence by means of cross-border and cross-sector mobility
  

Tema(s)

• MSCA-IF-2014-EF - Marie Skłodowska-Curie Individual Fellowships (IF-EF)
  

Régimen de financiación

MSCA-IF-EF-ST - Standard EF

Convocatoria de propuestas

H2020-MSCA-IF-2014

Coordinador

CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS

• Aportación neta de la UEn: € 185 076,00
• Dirección: RUE MICHEL ANGE 3 ; 75794 PARIS ; Francia
• Tipo de actividad: Research Organisations
• Coste total: € 185 076,00