IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Structural studies on a two-component system activated by blue light in Brucella abortus.
Autor/es:
KLINKE S., RINALDI J. J., SYCZ G., PARIS G. & GOLDBAUM F. A.
Lugar:
Carlos Paz
Reunión:
Congreso; XLII Reunión Anual de la Sociedad Argentina de Biofísica; 2013
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
Brucella abortus is an intracellular pathogen that causes a worldwide zoonosis called brucellosis, an endemic disease that causes abortion and infertility in cattle with consequent huge economic losses. One of the projects in our lab focuses on the study of a particular two-component signal transduction system (TCS) in Brucella that is activated by blue light and was shown to be a key virulence factor [1]. This TCS is composed by (i) the sensor histidine kinase LOV-PAS-HK, which is a three-domain protein able to sense blue light through a bound FMN molecule, and (ii) two cognate response regulators called PhyR and CheY. In this talk, we will present our latest results regarding the structural description of this system using protein X-ray crystallography. Explicitly, we were able to solve the crystal structure of the isolated LOV [2] and HK domains in the sensor histidine kinase, as well as the structure of the response regulator PhyR.We will also describe our present strategies for the resolution of multi-domain constructs and complex structures. To finish, we will show the technical aspects of synchrotron radiation application for fast diffraction data collection and automated structure solving of the proteins described here, according to our experience at the SOLEIL synchrotron in France. Overall, the structural information on this TCS, complemented with biochemical studies that are being performed in our lab, correspond to an excellent starting point for the understanding of the signal transduction effect between the different domainsin LOV-PAS-HK and the general activation of histidine kinases. Acknowledgements: CONICET and MINCyT (funding). SOLEIL and Institut Pasteur Montevideo (access to X-ray data collection) [1] Swartz, T.E. et al. (2007) Science317, 1090-1093. [2] Rinaldi, J.J. et al. (2012) J. Mol. Biol.420, 112-127