Accueil > Research > Highlights > Archives > 2014
ERC Starting Grant 2014 for Hugues NuryThe European Research Council (ERC) has awarded a "Starting Grant" to Hugues Nury for his project of structural studies of mammalian Cys loop receptors.
During his PhD at IBS, Hugues Nury studied mitochondrial membrane protein structures. He specialized in bacterial Cys-loop receptors during a first postdoc at the Institut Pasteur (France) in the laboratories of Corringer and Delarue. He then moved on to work on the mouse 5-HT3 serotonin receptor at the EPFL (Switzerland) during a second postdoc in the laboratory of Vogel. Since 2013, Hugues works at IBS and recently deciphered the X-ray structure of serotonin receptor. This collaborative study, published in Nature last year, paves the way for the design of new drugs against nausea, a main side effect of chemotherapy and anesthesia. What is this project about ? Keywords : neurotransmission, ionic channels, serotonine receptor Amount of the award : €1.5 million for five years Mini CV : |
Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan
Atomic model of a cell-wall cross-linking enzyme in complex with an intact bacterial peptidoglycan. Paul Schanda, Sebastien Triboulet, Cedric Laguri, Catherine M. Bougault, Isabel Ayala, Morgane Callon, Michel Arthur and Jean-Pierre Simorre. JACS |
A quartz crystal microbalance method to study the reducing end functionalization of glycosaminoglycans
Stable and Terminally Functionalized Glycosaminoglycan Conjugates. Thakar D., Migliorini E., Coche-Guerente L., Sadir R., Lortat-Jacob H., Boturyn D., Renaudet O., Labbe P., and Richter R.P. Chem. Comm. 50, 15148-15151 (2014) |
Finding your better half : specific oligomerization of a large 500 kDa macromolecular machine optimizes its enzymatic performance
Small angle neutron scattering reveals the assembling mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase. Appolaire A, Girard E, Colombo M, Durá MA, Moulin M, Härtlein M, Franzetti B and Gabel F. Acta Crystallographica Section D-Biological Crystallography ;70(Pt 11):2983-93 |
New opportunities for data mining in structural biologyPhylogenomic analysis of extreme halophilic Archaea sheds light on osmoadaptive mechanisms : new opportunities for data mining in structural biology.
Phylogenetically Driven Sequencing of Extremely Halophilic Archaea Reveals Strategies for Static and Dynamic Osmo-response. Erin A. Becker, Phillip M. Seitzer, Andrew Tritt, David Larsen,Megan Krusor, Andrew I. Yao, Dongying Wu, Dominique Madern, Jonathan A. Eisen, Aaron E. Darling, Marc T. Facciotti. Plos Genetics ;10(11) |
Unexpected radical reaction on tryptophan by NosL : H-abstraction from the amino N atom
Crystal Structure of Tryptophan Lyase (NosL) : Evidence for Radical Formation at the Amino Group of Tryptophan. |
Overview of the 2014 Science FairAfter a break in 2013, due to the relocation of the institute,, IBS scientists resumed their participation in the Science Fair with a guided tour for general public and workshops for CM2 classes. For the International Year of Crystallography, the Science Fair 2014 was particularly rich and original in Isere, from 26 September to 19 October 2014. The IBS could not miss this event and proposed two initiatives : On October 02 and 03, a hundred pupils were invited to participate in one of three workshops (short experiments involving proteins and DNA) dedicated for primary schools.
On October 18, two visits were organized on EPN Campus. A guided tour entitled "At the heart of the living molecules" was organized in the IBS building by scientists from IBS, EMBL, UVHCI and ESRF They animated three workshops about NMR, microbiology and crystallography. Inside a marquee at the entry of the campus, crystallography activities were also put on for people of all ages. Visitors were also welcomed elsewhere on the EPN campus, at the ESRF and the ILL.
In total about 40 volonteers were involved on both events to share the great pleasure of discovery with 250 people. Do not miss this crystallographic flashmob, a performance organized specially for the Science Fair 2014 in Grenoble. |
Frank Gabel nominated as co-director of the HERCULES schoolFrank Gabel (IBS/ELMA) has been nominated as co-director of the HERCULES school for the biology session, together with the new general director Vincent Favre-Nicolin (CEA), and the co-directors Michael Krisch (ESRF) and David Djurado (CNRS). The HERCULES school provides training for students, postdoctoral and senior scientists from European and non-European universities and laboratories, in the field of Neutron and Synchrotron Radiation for condensed matter studies Please note that the registration to the 2015 HERCULES session is opened until October 15th, 2014. To know more. |
Structural study of a protein-RNA complex involved in the regulation of gene expression in Drosophila sex chromosomes
Structural basis for the assembly of the Sxl–Unr translation regulatory complex. Janosch Hennig, Cristina Militti, Grzegorz M. Popowicz, IrenWang, Miriam Sonntag, Arie Geerlof1, Frank Gabel, Fatima Gebauer & Michael Sattler. |
Structure of a bacterial α2-macroglobulin reveals mimicry of eukaryotic innate immunity
Structure of a bacterial α2-macroglobulin reveals mimicry of eukaryotic innate immunity. |
X-ray structure of the mouse serotonin 5-HT3 receptorFor the first time the X-ray structure of serotonin receptor was deciphered. The study, published online in Nature on August 03, 2014, paves the way for the design of new drugs against nausea, a main side effect of chemotherapy and anesthesia. It was conducted by IBS researchers in collaboration with researchers from the laboratory Architecture and Function of Biological Macromolecules, Swiss researchers and the participation of Théranyx. X-ray structure of the mouse serotonin 5-HT3 receptor. Ghérici Hassaine, Cédric Deluz, Luigino Grasso, Romain Wyss, Menno B. Tol, Ruud Hovius, Alexandra Graff, Henning Stahlberg, Takashi Tomizaki, Aline Desmyter, Christophe Moreau, Xiao-Dan Li, Frédéric Poitevin, Horst Vogel and Hugues Nury. Nature, en ligne le 3 août 2014. |
Observing transient states of proteins at atomic résolutionThe three-dimensional shape of a protein determines its function. In many cases, however, the conformational states that are actually relevant for function are only transient and populated to a small extent at any given time, and therefore difficult to grasp by existing methods. A new method based on solid-state NMR spectroscopy, developed by researchers at IBS, allows detecting transient protein states even in large or insoluble proteins. Proteins fulfill an impressively wide range of tasks in the cell, and their function is tightly bound to their shape. Biologists use techniques such as Nuclear Magnetic Resonance (NMR) to determine these structures. But proteins do not have only one rigid conformation, but they continuously exchange between different conformations. In many cases proteins perform their tasks within milliseconds or even faster, such that relevant conformational states may only last for a tiny fraction of a second, and in a given sample only a small part of the molecules may be in some of these functional states. NMR spectroscopic techniques developed over the last decade are able to provide information about such short-lived states for proteins in solution, even though they are transient and rare, but extending this to large or insoluble proteins (such as membrane proteins) remained so far very challenging. Researchers from IBS Grenoble, in collaboration with Forschungszentrum Jülich (Germany) have developed a new method that overcomes these limitations and allows studying proteins in the solid state, which opens the possibility to see motion in proteins that were so far out of reach. The methodology provides insight into these rare and transient states, in terms of their structural changes, as well as into the kinetics and thermodynamics of these dynamic fluctuations. The techniques was first demonstrated on a well-established protein, ubiquitin. It had been known before that this protein exists in two slightly different conformational states, as seen in different crystal structures. With the new technique, the IBS researchers could show that both states co-exist in the crystal, i.e. the protein constantly “hops” from one state to the other, making it thereby able to expose conformations that are preorganized for their binding partners. The method, which is currently being applied to large challenging systems, is expected to also help understanding how potentially medically relevant proteins, such as membrane receptors or large enzymes function.
Probing Transient Conformational States of Proteins by Solid-State R11 Relaxation-Dispersion NMR Spectroscopy.Peixiang Ma, Jens D. Haller, J-r-my Zajakala, Pavel Macek, Astrid C. Sivertsen, DieterWillbold, J-er-ome Boisbouvier, and Paul Schanda. Angew Chem Int Ed Engl. 2014 Apr 22 ;53(17):4312-7. doi : 10.1002/anie.201311275. Epub 2014 Mar 18. |
Official inauguration of the new IBS buildingFriday 21 February saw the official opening of the new IBS building which was funded by local and regional authorities within the framework of a CPER contract (Contrat de Projets Etat-Région) and the Plan Campus.
Built on the EPN Science Campus in the heart of Giant, the new 5600 m2 building offers a unique environment for researchers to decipher the living world at a molecular level. The IBS’s location close to its PSB partners (Partnership for Structural Biology) allows access to cutting-edge facilities and constitutes a further step in the development of the region as an International centre of excellence for structural biology. As 2014 has been declared by Unesco the "International Year of Crystallography", the IBS groups now have at their disposal a unique environment for furthering knowledge about the molecular and cellular architecture and dynamics of living organisms.
|