Unveiling the structure of pathogenic macromolecular machines using integrative dynamic modeling
Event details
| Date | 11.12.2013 |
| Hour | 12:15 › 13:10 |
| Speaker |
Prof. Matteo Dal Peraro Bio: Matteo Dal Peraro graduated in Physics at the University of Padua in 2000. He obtained his Ph.D. in Biophysics at the International School for Advanced Studies (SISSA, Trieste) in 2004. He then received postdoctoral training at the University of Pennsylvania (Philadelphia) under the guidance of Prof. M. L. Klein. He was nominated Tenure Track Assistant Professor at the EPFL School of Life Sciences in late 2007. His research at the Laboratory for Biomolecular Modeling (LBM), within the Interfaculty Institute of Bioengineering (IBI), focuses on the multiscale modeling of large macromolecular systems. |
| Location | |
| Category | Conferences - Seminars |
Proteins often assemble in large macromolecular complexes to achieve a specific biological task. Unfortunately, owing to their size and complexity, these structures are difficult to determine at atomistic resolution, preventing thus a complete understanding of their mechanism of action.
In this talk I will present the effort of my laboratory to develop novel ways to predict the structure and function of large biological assemblies. To this end, we established a new approach that uses swarm intelligence optimization guided by experimental-based restraints to characterize quaternary protein structure accounting for native dynamics.
Using this integrative strategy we were able to reveal the assembly mechanism of aerolysin, a bacterial pore-forming toxin that produces heptameric pores at the target membrane by a concerted swirling motion of its components. In a second study, we determined the basal body structure of Yersinia type III secretion system, discovering how its flexibility is critical for adapting to thickness variations at the periplasmic space.
The native dynamics of individual components emerges, in these studies, as the key determinant to define the architecture and understand the function of large multi-protein complexes. Therefore, the ability of our approach to integrate protein dynamics with sparse experimental data is a promising step toward the molecular characterization of large pathogenic systems and the design of specific therapeutic strategies.
In this talk I will present the effort of my laboratory to develop novel ways to predict the structure and function of large biological assemblies. To this end, we established a new approach that uses swarm intelligence optimization guided by experimental-based restraints to characterize quaternary protein structure accounting for native dynamics.
Using this integrative strategy we were able to reveal the assembly mechanism of aerolysin, a bacterial pore-forming toxin that produces heptameric pores at the target membrane by a concerted swirling motion of its components. In a second study, we determined the basal body structure of Yersinia type III secretion system, discovering how its flexibility is critical for adapting to thickness variations at the periplasmic space.
The native dynamics of individual components emerges, in these studies, as the key determinant to define the architecture and understand the function of large multi-protein complexes. Therefore, the ability of our approach to integrate protein dynamics with sparse experimental data is a promising step toward the molecular characterization of large pathogenic systems and the design of specific therapeutic strategies.
Links
Practical information
- Informed public
- Free
Organizer
- Dean's Office, School of Life Sciences
Contact
- Dr H. Hirling / M. Mary