Highlights

2022 Scientific Day and celebration of the IBS 30th Anniversary

2022 marks the 30th anniversary of the Institut de Biologie Structural and it was celebrated on June 16, 2022. For this special occasion, our annual scientific day took place in the Minactec amphitheater with retrospectives to honor three decades of achievement, as well as a part dedicated to current issues and perspectives. A particular focus was presented on crystallography (after a focus on NMR in 2019 and electron microscopy in 2021). In order to share these presentations with our academic and industrial partners, videos of some key moments will be put online on the IBS Youtube channel by the fall.

A poster session was also proposed during lunch, and news from former PhD students were broadcasted through videos. The IBS 2022 Young Researcher Prize was awarded to Benoit Arragain who performed his thesis in the MEM group on the Structural and functional analysis of Bunyavirales replication and transcription. Elda Bauda (second yeay PhD student in the ) received the Flash/Poster Prize for her work on the architecture of SpoIIIA-SpoIIQ, a nanomachine involved in bacterial sporulation.

The closing conference "From Curiosity to Perseverance" was given by two speakers from the Observatoire des Sciences de l’Univers de Grenoble and was dedicated to a decade of research on the surface of Mars.

To celebrate this 30th anniversary in a friendly atmosphere, a festive dinner was organized on the EPN campus for the IBS staff with games and musical animations.

Happy 30th Anniversary IBS !

Diner anniversaire / Celbration Diner

New issue for the IBS Newsletter

Find the June 2022 issue (in french only).

Radical chemistry : how radical SAM enzymes control it

Radical chemistry uses high-energy intermediates to carry out difficult reactions or even ones impossible to perform by the so-called polar chemistry. In nature, these reactions are fine-tuned by the structural environment within dedicated enzymes. Radical SAM proteins use an iron-sulfur cluster and S-adenosyl-L-methionine to initiate several radical reactions. These metalloproteins are notably involved in the biosynthesis of numerous cofactors and in the modification of peptides with antibiotic properties. The crystal structure of ThiH, involved in the anaerobic synthesis of vitamin B1, allowed us, by combining structural analysis and theoretical calculations, to understand how the substrate is recognized by the protein and how it is activated. In particular, hydrogen atom transfer is facilitated by a tunnel effect which allows the lowering of the activation barrier.
In conclusion, this work showed how a sum of small changes allowed to modify both the substrate selectivity and the specificity of a chemical reaction within this important family of proteins, thus paving the way to future molecular engineering approaches for more extensive use of these proteins as a biotechnological tool.

L-tyrosine-bound ThiH structure reveals C-C bond break differences within radical SAM aromatic amino acid lyases. Amara P, Saragaglia C, Mouesca JM, Martin L, Nicolet Y. Nature Communications ; 13(1):2284

Contact : Yvain Nicolet( IBS/Metalloproteins group)