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Dr. Kristina Djinovic Carugo Doctoral Degree in Chemistry, Univ. Ljubljana, Slovenia; 1992. Post-Doctoral Research Associate, Dept. Genetics and Microbiology, Univ. Pavia, Italy, 1992-1995. Post-Doctoral Research Associate (EMBO-Fellow), Structural and Computational Biology Programme, EMBL-Heidelberg, Germany; 1995-1997. Staff-Scientist in Structural and Computational Biology Programme, EMBL-Hedidelberg, Germany; 1997-1999. At Elettra since mid 1999
phone: +39-040-375 8059
Research Interests.Structural studies of metalloenzymes involved in denitrification and radical protection.
Denitrifying bacteria obtain metabolic energy by using
nitrogen-oxidised compounds instead of oxygen as terminal electron
acceptors in anaerobic respiration. Understanding of denitrification is
of extreme importance for the removal of toxic compounds (e.g. N2O).
The information on structural and mechanistic properties of enzymes
will enable the design of biomimetic organic compounds that are capable
of removing of toxic compounds from waste water streams.
Figure of nitrous oxide reductase monomer.
Superoxide dismutases are ubiqitous enzymes that protect organism from
superoxide radical. Structural studies on these enzymes are focused on
two fields: Structural Biology of Cytoskeleton. Cytosol is the part of the cytoplasm that is not contained in membrane-limited organelles. The cytosol of eukaryotic cells contains an array of fibrous proteins collectively called the cytoskeleton. Among these fibers are the microfilaments built of protein actin, microtubules built of tublin, and intermediate filaments built of one or more protein subunits. Cytoskeletal fibers give the cell strength and rigidity, and are also involved in cell motility. The organization of the cytoskeleton is based on the principle that large complex structures are built from small, simple components. The theme of assembling complicated structures from simple components is carried out by cross-linkages of cytoskeletal fibers into structure like bundle, networks and gel-like lattices. The cell takes its shape by bonding the plasma membrane to these protein supports. Actin filaments participate in biological processes ranging from movements of protozoa to muscle contraction. Some of there processes including muscle contraction and cytokinesis require motor proteins of the myosin family, which move along actin filament tracks. Other motile processes, like extension of pseudopods are driven by the regulated assembly and disassembly of a network of actin filaments. The focus of this research lies in:
I) proteins involved in binding to actin filaments, both in muscle and
cell-cytoskeleton; proteins with different cell localisation but
similar function are currently under study. Actin binding region of
human alpha-actinin has recently been solved. Figure of actin binding region of human alpha-actinin. II) regulation of muscle contraction III) proteins involved in focal contacts and attachment to plasma membrane
The research in this field is expected to evolve from the study of a
single protein towards structural studies of macromolecular assemblies.
Namely, understanding of the events and interactions in focal contacts
as revealed from the cell-biology studies has become detailed enough to
identify specific interacting partners. MAD experiments at long wavelenghts. The growth of macromolecular crystal structure determination and the increasing number of experiments performed at synchrotron facilities require that more efficient use is made of these infrastructures. Obtaining the phases of the structure factors is a limitation in structure determination second only to obtaining crystals. The multiple-wavelength anomalous dispersion (MAD) and optimized single isomorphous replacement with anomalous signal (SIRAS) techniques offer a general method of overcoming this problem. It is therefore desirable to perform diffraction experiments at energies close to the absorption edges of a wide variety of elements. We therefore commited ourselves to offer to the European crystallographic user community:
Job Openings.
SISSA PhD programme in Structural and Functional genomics: www.sissa.it External Funding.European Union Fifth Framework (EU): EU RTD project: Extension of MAD capabilities at synchrotron infrastructures EU Network: The structure and function of mammalian cytoskeleton
EU Infrastructure cooperation network: European Macromolecular
Crystallography Network Selected Publications.Bordo, D., Djinovic, K. & Bolognesi, M. Conserved Patterns in the Cu, Zn Superoxide Dismutase Family.
J. Mol. Biol. (1994), 238, 366-386. Djinovic Carugo, K., Banuelos, S. & Saraste, M. Crystal Structure of a Calponin Homology Domain.
Nature Struct. Biol. (1997), 4, 175-179. Banuelos, S., Saraste, M. & Djinovic Carugo, K. Structural Comparison of Calponin Homology Domains: Implications for Actin Binding.
Structure (1998), 6, 1419-1431. Baraldi, E., Djinovic Carugo, K., Hyvoenen, M., Lo Surdo, P., Riley, A., Potter, B. & Saraste, M. Structure of the PH Domain from Brutonís Tyrosine Kinase in Complex with Inositol-(1,3,4,5)- tetrakisphosphate.
Structure (1999), 7, 449-460. Djinovic Carugo, K., Young, P., Gautel, M. & Saraste, M. Structure of the alpha-Actinin Rod: Molecular Basis for Crosslinking of Actin Filments.
Cell (1999), 98, 537-546. Brown, K, Djinovic-Carugo, K, Haltia, T., Cabrito, I., Saraste, M, Moura, J.J., Moura, I., Tegoni, M., & Cambillau, C. Revisiting the Catalytic CuZ Cluster of N2O Reductase: Evidence of a Bridging Inorganic Sulphur.
J. Biol. Chem. (2000), 275, 41133-41136. Weiss, M.S., Sicker, T., Djinovic-Carugo, K. & Hilgenfeld, R. On the Routine Use of Soft X-rays in Macromolecular Crystallography. Acta Cryst. D57, (2001), 689-695. |
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