Functional and small-angle X-ray scattering studies of a new stationary phase survival protein E (SurE) from Xylella fastidiosa - evidence of allosteric behaviour.
作者： Antonio M. Saraiva , Marcelo A. Reis , Susely F. Tada , Luciana K. Rosselli-Murai , Dilaine R. S. Schneider
DOI: 10.1111/J.1742-4658.2009.07390.X
关键词: Biochemistry 、 Tetramer 、 Nucleotidase 、 Open reading frame 、 ORFS 、 Biology 、 Cooperative binding 、 Protein secondary structure 、 Gene 、 Allosteric regulation
摘要: The genome data of bacterium Xylella fastidiosa strain 9a5c has identified several orfs related to its phytopathogenic adaptation and survival. Among these genes, the surE codifies a survival protein E (XfSurE) whose function is not so well understood, but functional assays in Escherichia coli revealed nucleotidase exopolyphosphate activity. In present study, we report XfSurE overexpression E. coli purification. overall secondary structure was analyzed by CD. Small-angle X-ray scattering gel filtration techniques demonstrated that oligomeric state solution tetramer. addition, kinetics experiments were carried out with monophosphate nucleoside substrates highly positive cooperativity. An allosteric mechanism involving torsion movements proposed explain cooperative behaviour XfSurE. This first characterization SurE enzyme from phytopathogen organism and, our knowledge, be described. Structured digital abstract • MINT-7262492: (uniprotkb:Q9PF20) bind (MI:0407) x ray (MI:0826) • MINT-7262504: molecular sieving (MI:0071)
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