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Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / BOISBOUVIER Jerome / BRUTSCHER Bernhard / FAVIER Adrien / SCHANDA Paul / Simorre Jean-Pierre

Latest research results

Detailed insight into dynamics in a 0.5 MDa-large enzyme from solid-state NMR. Diego’s paper is out in JACS.

An advanced isotope-labeling scheme along with proton-detected magic-angle spinning NMR provides very detailed views of motions of aromatic rings, down to 100 K, and over time scales spanning 8 orders of magnitude.
Find the manuscript HERE

Integrated NMR + EM structure determination published in Nature Communications : new method, new record !

Our latest preprint is out on the integrated structure determination from NMR and EM data. We have been able to assign, essentially to completion, the 12 x 39 kDa protein assembly TET2, the largest protein for which this such a detailed analysis has been achieved. We have developed a new approach, which jointly exploits NMR and EM data and which allowed to obtain a near-atomic-resolution structure from these data.
Find the manuscript HERE

On the cover of Cell : The mechanism of chaperones transporting membrane proteins in mitochondria

Latest research results {PNG}

The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones.
By integrating NMR with numerous other biophysical, structural and in-vivo approaches, we have provided a detailed picture of this highly dynamic chaperone complex. Details can be found HERE

The article has been hightlighted in the "Faculty of 1000"

27/9/2018

Structural investigation of a chaperonin in action

Many fundamental cellular functions are performed by large protein assemblies. This applies in particular to protein quality control, the process by which cells ensure the recycling or correct folding of their main constituents, in order to avoid the accumulation of poorly folded proteins, aggregates or fibrils. These large machineries - chaperones, proteases and peptidases - are complex and dynamic. The studies of such biological machines present a significant challenge, due to the very size of these particles, the complexity of their biological substrates and the structural rearrangements involved. IBS researchers have implemented an approach that combines site-specific nuclear magnetic resonance observation of very large proteins, enabled by advanced isotope labeling methods, with an in situ ATP regeneration system. Using this method, they provide functional insight into the 1-MDa large hsp60 chaperonin while processing client proteins. The results, published in Sciences Advances on September 19, 2018, reveal how the functional cycle of this complex assembly is regulated. This approach opens up new perspectives for directly studying the structures and mechanisms of various biological machines in action.
Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle. Mas G, Guan J-Y, Crublet E, Colas Debled E, Moriscot C, Gans P, Schoehn G, Macek P, Schanda P, Boisbouvier J. Science Advances 2018 September 19