Expression, Purification, Crystallization and X-Ray Crystallographic Analysis of MoDabb1 from Magnaporthe oryzae

Аннотация

Protein acetylation is one of the most common post-translational modifications. Many acetylated proteins in Magnaporthe oryzae play key roles in vegetative growth and pathogenicity. MoDabb1 from M. oryzae was also identified to be an acetylated protein, containing a Dabb domain with unknown function. To elucidate the function of this protein and the effect of acetylation on this protein, a native and selenomethionine-substituted MoDabb1 were expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using sitting-drop vapour-diffusion method. Crystals of native and selenomethionine-substituted protein were diffracted to a resolution of 1.74 and 1.98 Å and both belonged to the sp. gr. P4₂2₁2. Matthews coefficient analysis indicated two molecules in an asymmetric unit with a Vm value of 2.41 and a corresponding solvent content of 49.03%.