Emmanuel Levy

2020 Israel Award Winner — Faculty

Current Position:
Senior Scientist

Institution:
Weizmann Institute of Science

Discipline:
Biochemistry & Structural Biology

Recognized for: Combining computational models of protein structure derived from X-ray crystallography with protein engineering to provide reliable information about protein organization within cells.

Areas of Research Interest and Expertise: Structural Biology, Protein-Protein Interactions, Proteome Self-Assembly, Computational Biology

Previous Positions:

BSc, Evry University (Génopôle), France
MSc (1^st Year), Evry University (Génopôle), France
MSc (2^nd Year), Paris VII University, France
PhD, University of Cambridge, United Kingdom (Advisor: Dr. Sarah Teichmann)
Postdoctoral Fellow, University of Montreal, Canada (Advisor: Prof. Stephen Michnick)

Research Summary:

Emmanuel Levy, PhD, investigates the principles of protein assembly and self-organization in the proteome. The proteome is the entire set of proteins that can be expressed at a given time, and even for a simple organism like baker’s yeast—the model organism he studies in his laboratory—the proteome involves a choreography between tens of millions of proteins. The task of understanding how these millions of proteins assemble and work together to support life is extraordinarily complex. Levy is taking an interdisciplinary approach to address this challenge and has revealed basic principles of this choreography, at multiple scales. At the most fundamental level, protein assembly takes place by homo-oligomerization, in which identical copies of a protein become arranged symmetrically into higher-order structures that can possess functionality. These so-called quaternary structures can be predicted using a computational strategy that Levy devised for many thousands of proteins of known structure. Zooming-out one level, he predicted and demonstrated experimentally that symmetric homo-oligomers are highly susceptible to forming infinitely long polymers by mutation. These findings shift the paradigm of how quickly new protein assemblies can emerge during evolution. Zooming out yet another level, Levy developed effective methods for the systematic tagging of proteins in yeast cells and their visualization. Levy’s research, which bridges atomic and cellular scales, generates original concepts and powerful tools for probing and grasping the molecular “sociology” of proteins inside living cells.

"The underlying beauty of how matter organizes in living cells is both deeply inspiring and frightening, due to the sheer complexity of the mechanisms involved. Receiving the Blavatnik Award is an immense honor, encouraging me to pursue my work with the ambition that in the future, it will be possible to grasp the inner workings of a cell to atomic detail. I am most grateful to my present and past group members for their amazing ideas and hard work, to my mentors and colleagues for their continuous and inspiring support, and to my family for providing what life is all about, beyond the molecules."

Key Publications:

1. H. Garcia-Seisdedos, C. Empereur-Mot, N. Elad, E.D. Levy. Proteins Evolve on the Edge of Supramolecular Self-assembly. Nature, 2017.

2. S. Dey, D.W. Ritchie, E.D. Levy. PDB-wide Identification of Biological Assemblies from Conserved Quaternary Structure Geometry. Nature Methods, 2017.

3. M. Meurer, Y. Duan, E. Sass, I. Kats, K. Herbst, B.C. Buchmuller, V. Dederer, F. Huber, D. Kirrmaier, M. Stefl, K. Van Laer, T.P. Dick, M.K. Lemberg, A. Khmelinskii, E.D. Levy, M. Knop. Genome-wide C-SWAT Library for High-throughput Yeast Genome Tagging. Nature Methods, 2018.

4. H. Garcia-Seisdedos, J.A. Villegas, E.D. Levy. Infinite Assembly of Folded Proteins in Evolution, Disease, and Engineering. Angewandte Chemie International Edition, 2019.

Other Honors:

In the Media:

Weizmann Wonder Wander - Lego Proteins Revealed

Human Fronteir Science Program - Playing LEGO with proteins

nanowerk - Self-assembling protein complexes could provide scaffolding for nanostructures

Website