IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Crystallization and preliminary X-ray characterization of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris pv. campestris (Conferencia Invitada)
Autor/es:
SEBASTIÁN KLINKE; LISANDRO OTERO; JIMENA RINALDI; SANTIAGO SOSA; FERNANDO A. GOLDBAUM; HERNÁN R. BONOMI
Lugar:
Montevideo
Reunión:
Congreso; Primer Encuentro de la Red Uruguaya de Cristalografía (RUCr); 2014
Institución organizadora:
Red Uruguaya de Cristalografía (RUCr)
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 many bacterial phytochromes share a common architecture consisting of an N-terminal photosensory module (PAS2-GAF-PHY domains) and a C-terminal variable output module [1, 2, 3]. 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 (Fig. 1). A complete native X-ray diffraction dataset was collected to a maximum resolution of 3.25 Å at the SOLEIL Synchrotron. Crystals belong to the space group P43212 with unit-cell parameters a = b = 103.94, c = 344.57 Å, and a dimer in the asymmetric unit. Refinement is underway after solving the structure by molecular replacement.[1] M.E. Auldridge, K.T. Forest, Critical reviews in biochemistry and molecular biology, 46 (2011) 67-88.[2] N.C. Rockwell, J.C. Lagarias, Chemphyschem: a European journal of chemical physics and physical chemistry, 11 (2010) 1172-1180.[3] R.D. Vierstra, J. Zhang, Trends in plant science, 16 (2011) 417-426.