IIBBA   05544
INSTITUTO DE INVESTIGACIONES BIOQUIMICAS DE BUENOS AIRES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
A new phosphatase from an antarctic bacterium: molecular basis of cold adaptation mechanism
Autor/es:
ARAN M; SMAL C; GALLO M; PELLIZZA L; CICERO D
Lugar:
Mendoza
Reunión:
Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Bioquímica y Biología Molecular; 2012
Institución organizadora:
SAIB
Resumen:
A new bacterial strain designated as JUB59 was isolated from the Antarctic sea surface and grouped into the Flavobacteriaceae family. The bacterium was identified as a new species within the genus Bizionia and named Bizionia argentinensis (BA). Its genome was recently sequenced and represents an important source for the discovery of new proteins with biological activity at low temperatures. In order to structurally characterize a group of proteins of unknown function of BA, we carried out a method based on the selection of protein targets by NMR. By this method we were able to select proteins that given its solubility and folding became good candidates for structural determinations. Here, we present the solution structure of one of the selected targets, the protein BA42,revealing a previously unknown sequence/structure pair. By comparing the 3D structure of BA42 with existing databases, we characterize the phosphatase activity in vitro. This activity was dependent on divalent ions, particularly Mg2+. We also identified the key residues involved in the active site: E5 and K37. A smaller number of interactions and a more flexible structure of the active site, compared with the mesophilic counterpart, may explain the molecular basis of the cold adaptation mechanism.