Maltose Binding Protein (MBP) is a well-studied protein derived from Escherichia coli (E. coli). It plays a crucial role in the maltose/maltodextrin system of E. coli, which is responsible for the uptake and efficient catabolism of maltodextrins . MBP is widely used in recombinant protein expression systems due to its ability to enhance the solubility and proper folding of fusion proteins .
MBP is encoded by the malE gene in E. coli. The malE gene produces a precursor polypeptide consisting of 396 amino acid residues, which is then processed to yield the mature MBP with 370 residues . The mature form of MBP does not contain any cysteine residues and is a monomeric protein .
The protein is divided into two distinct globular domains connected by three short polypeptide segments. These domains are separated by a deep groove that contains the maltose/maltodextrin binding site . Binding of maltose induces a significant conformational change in MBP, closing the groove through a rigid motion of the two domains around the linking polypeptide hinge .
MBP is exported into the periplasmic space of E. coli. The NH2-terminal extension, also known as the signal peptide, plays a dual role: it slows down the folding of the newly synthesized polypeptide and directs it to the membrane and SecYEG translocon . Once folded, the precursor can no longer enter the translocation pathway .
MBP is extensively used as a fusion partner in recombinant protein expression systems. It is particularly valuable for increasing the solubility of recombinant proteins expressed in E. coli . The protein of interest is often expressed as an MBP-fusion protein, which helps prevent aggregation and enhances proper folding . The exact mechanism by which MBP increases solubility is not fully understood .
MBP fusion proteins are widely used in various applications, including protein purification, structural studies, and functional assays. The use of MBP as a fusion partner offers several advantages: