CONICET | Buscador de Institutos y Recursos Humanos

RINALDI, JIMENA; GUNAWARDANA, SEMINI ; YANG, XIAOJING; SHIN, HEEWHAN; CERUTTI, MARÍA LAURA; GOLDBAUM, FERNANDO A.; FERNÁNDEZ, IGNACIO; OTERO, LISANDRO H.; KLINKE, SEBASTIÁN

Lugar:

Bucaramanga

Reunión:

Congreso; IV Reunión de la Asociación Latinoamericana de Cristalografía; 2019

Institución organizadora:

Asociación Latinoamericana de Cristalografía

Resumen:

The pathogenic bacterium Brucella abortus codesfor a multi-domain cytoplasmic histidine kinase called LOV-HK, which is a keyblue light-activated virulence factor in this microorganism, and a member of atwo-component system involved in the bacterial general stress response. It hasbeen shown that the exposure of Brucella to visible light results in higherlevel of bacterial replication in the host cells, and that this effect ismediated by LOV-HK. Brucella LOV-HK is a dimeric protein that comprises anN-terminal blue-light sensor LOV domain, a central PAS domain with unknownfunction and a C-terminal histidine kinase HK domain[1, 2]. The mechanism ofactivation of this protein, and of sensor HK sin general, is not fullyunderstood. To address this challenge, we solved the crystal structure ofseveral multi-domain constructs of the protein in dark and illuminated states,including the full-length light-activated version at 3.25 Å resolution [3]. Theanalysis and comparison of these three-dimensional models allowed us to proposea model for the activation of this crucial system in Brucella, which will bepresented in this talk