21 June 2023
Europe/Rome timezone

Small Angle X-ray Scattering (SAXS) in combination with other complementary techniques to tackle challenging protein structures

21 Jun 2023, 14:30
15m

Speaker

Dr Dritan Siliqi (IC-CNR)

Description

Small Angle X-ray Scattering (SAXS) is widely used in the study of biomolecules, providing valuable insights into their structural properties and behavior in solution. SAXS is particularly suitable for investigating biomolecules' overall shape, size, conformation, and flexibility, including proteins, nucleic acids, and complexes. In the case of proteins, SAXS can provide information about their tertiary and quaternary structure, domain organization, and overall shape. SAXS is also useful for studying protein-protein interactions and the assembly of biomolecular complexes. One of the advantages of SAXS in studying biomolecules is its ability to analyze molecules in solution under near-physiological conditions. This allows for the investigation of biomolecular behavior in their native state, providing insights into their dynamics and conformational changes. Small Angle X-ray Scattering (SAXS) is often combined with other complementary techniques, such as X-ray Crystallography, Nuclear Magnetic Resonance (NMR) Spectroscopy, Electron Microscopy (EM), Mass Spectroscopy, Molecular Dynamic simulations (DM) and protein-protein docking, to tackle challenging protein structures and obtain a more comprehensive understanding of their properties. Results obtained from the study of proteins and their complexes involved in the mechanism of diseases such as Shwachman Diamond [1-2] and Jalili [3] syndromes, and tuberculosis [4], will be shown.

  1. Stepensky, P.; Chacon-Flores, M.; Kim, K.H.; Abuzaitoun, O.; Bautista-Santos, A.; Simanovsky, N.; Siliqi, D.; Altamura, D.; Mendez-Godoy, A.; Gijsbers, A.; et al. Mutations in EFL1, an SBDS partner, are associated with infantile pancytopenia, exocrine pancreatic insufficiency and skeletal anomalies in a Shwachman-Diamond like syndrome. J. Med. Genet. 2017, 54, 558–566 .
  2. Gijsbers, A., Montagut, D. C., Mendez-Godoy, A., Altamura, D., Saviano, M., Siliqi, D., & Sanchez-Puig, N. Interaction of the GTPase elongation Factor Like-1 with the Shwachman-Diamond Syndrome protein and its missense mutations. International Journal of Molecular Sciences, 2018, 19(12), 4012
  3. Paula Gimenez-Mascarell, Iker Oyenarte, Irene Gonzalez-Recio, Carmen Fernandez-Rodriguez, Maria Angeles Corral-Rodriguez, Igone Campos-Zarraga, Jorge Simon, Elie Kostantin, Serge Hardy, Antonio Diaz Quintana, Mara Zubillaga Lizeaga, Nekane Merino, Tammo Diercks, Francisco J. Blanco, Irene Diaz Moreno, Maria Luz Martinez- Chantar, Michel L. Tremblay, Dominik Mueller, Dritan Siliqi, and Luis Alfonso Martinez-Cruz. Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4. International Journal of Molecular Sciences, 2019, 20(24).
  4. Gijsbers, A, Eymery, M., Gao, Y., Menart, I., Vinciauskaite, V., Siliqi, D; Peters, P.J; McCarthy, A. and Ravelli, R.B.G Ravelli. Structure of the EspB-EspK complex of M. tuberculosis: the non-identical twin of the PE-PPE-EspG secretion mechanism. Journal of Biological Chemistry,2023, 299(1) 102761

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