INVESTIGADORES
KLINKE Sebastian
congresos y reuniones científicas
Título:
Crystallization and preliminary X-ray characterization of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris pv. campestris (Poster)
Autor/es:
SEBASTIÁN KLINKE; LISANDRO OTERO; JIMENA RINALDI; SANTIAGO SOSA; FERNANDO A. GOLDBAUM; HERNÁN R. BONOMI
Lugar:
Sierra de la Ventana, Pcia Buenos Aires
Reunión:
Congreso; XLIII Reunión Anual de la Sociedad Argentina de Biofísica; 2014
Institución organizadora:
Sociedad Argentina de Biofísica (SAB)
Resumen:
Phytochromes give rise to the largest photosensor family known to date. However, they are underrepresented in the Protein Data Bank. Plant, cyanobacterial, fungal and bacterial phytochromes share a canonical architecture consisting of an N-terminal photosensory module (PAS2-GAF-PHY domains) and a C-terminal variable output module. The bacterium Xanthomonas campestris pv. campestris, a worldwide agricultural pathogen, codes for a single bacteriophytochrome (XccBphP) that holds this canonical architecture, bearing a C-terminal PAS9 domain as the output module. Full-length XccBphP was cloned, expressed and purified to homogeneity by nickel-NTA affinity and size exclusion chromatography and then crystallized at room temperature bound to its cofactor biliverdin. A complete native X-ray diffraction dataset was collected to a maximum resolution of 3.25 A. Crystals belong to the space group P43212 with unit-cell parameters a = b = 103.94, c = 344.57 A, and a dimer in the asymmetric unit. Refinement is underway after solving the structure by molecular replacement [1].This work was supported by CONICET, ANPCyT, MINCyT and the SOLEIL Synchrotron (France).1- Klinke, S. et al. & Bonomi, H.R. Acta Crystallographica Section F: Structural Biology Communications. 2014. In press.