Preliminary Diffraction Analysis and C-Lobe Flexibility of Maltose Binding Protein

Maltose binding protein (MBP) is essential for carbohydrate transport and metabolism in all types of cells and is characterized by its high solubility and robust expression.Consequently, it is widely used to increase the solubility of recombinant proteins expressed in Escherichia coli.MBP exists in a stable monomeric state with two globular lobes: the N-lobe and the C-lobe at each end.In this study, we identified the structural characteristics of MBP from two different crystal forms.Upon comparing these structures, we observed distinct structural features between the two lobes: a stable N-lobe and a flexible C-lobe.These contrasting structural characteristics likely contribute to the high solubility of fused proteins and the stable interactions facilitated by the flexibility of the C-lobe.