Biochemistry, Biophysics & Structural Biology Department

Biochemistry, Biophysics and Structural Biology Department

Head: 

Julie Ménétrey

Deputy  heads:

    Benoit D’Autréaux 

Virginie Gervais 

From Atoms to Function : Decoding How Macromolecular Structures and Dynamics Orchestrate Life

Focus

The B3S teams study soluble and membrane protein assemblies involved in major biological processes of eukaryotic and bacterial cells. 

Our aim is to  understand the molecular mechanisms of biological structures and biochemical reactions at different scales, from electrons and protons via atoms and molecules to multicellular organisms. Successfully introduced new technologies to promote product innovation and upgrades.

Approaches

Biochemical reactions, interactions and enzymatic processes, including large conformational changes and rearrangements within proteins and their complexes, are often initiated by a transfer of subatomic particles – electrons and protons. Studying the atomic structures of proteins with and without ligands can for example help determine how the structure of the active site enables an enzyme to perform its activity.

At molecular scales, biochemical and biophysical analyses as well as structure determination of protein-protein, or protein-nucleic acid complexes, helps in describing the interaction of biological assemblies and understanding biochemical reactions.  In vitro reconstitution of cellular functions leads to an understanding of the regulation of complex processes in vivo.

Research groups

Publications

3888256 B3S 1 chicago-author-date 5 date desc year 36406 https://www.i2bc.paris-saclay.fr/wp-content/plugins/zotpress/
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Gong, Xiaodi, Marlena Pożoga, Jean-Baptiste Boyer, et al. 2026. “The Ribosome-Associated N-Terminal Acetyltransferase B Coordinates Global Proteostasis and Autophagy in Plants by Creating Ac/N-Degrons.” Nature Communications 17 (1): 3116. https://doi.org/10.1038/s41467-026-71208-2.
Khan, Mantasha, Nathalie Lejal, Fanny Boursin, et al. 2026. “A Spike-Binding Protein as a Versatile Tool to Detect and Inhibit Transmissible Gastroenteritis Virus.” Virology 619 (March): 110887. https://doi.org/10.1016/j.virol.2026.110887.
Marouf, Zahra, Carine Tellier-Lebegue, Matthieu Glousieau, et al. 2026. “The tRNA Moieties of Both Aminoacyl-tRNA Substrates of a Cyclodipeptide Synthase Share a Common Binding Site, as Revealed by RNA Microhelices Mimicking tRNA Acceptor Arms.” Nucleic Acids Research 54 (6): gkag307. https://doi.org/10.1093/nar/gkag307.
Collotta, Giulio, Marco Gatti, Irina-Maria Ungureanu, et al. 2026. “USP7 Deubiquitinase Stabilizes FAN1 to Support DNA Crosslink Repair and Suppress CAG Repeat Expansion.” Nature Communications, ahead of print, March 6. https://doi.org/10.1038/s41467-026-70051-9.
Combet, Sophie, Raphael Dos Santos Morais, Audrey Comte, et al. 2026. “Weak Protein-Bicelle Binding Quantification via Surface-Based DNA Nanolevers.” European Biophysics Journal: EBJ, ahead of print, March 2. https://doi.org/10.1007/s00249-026-01829-4.

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