Maltose-binding protein

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Maltose-binding protein

Maltose-binding protein structure

Maltose-binding protein (MBP) is a protein that plays a crucial role in the transport and metabolism of maltose in bacteria. It is a periplasmic binding protein that binds specifically to maltose, facilitating its uptake into the cell. MBP is commonly used in molecular biology and biotechnology applications due to its high affinity for maltose and its stability.

Structure

MBP is a single polypeptide chain consisting of approximately 370 amino acids. It has a characteristic periplasmic binding protein fold with two domains connected by a hinge region. The N-terminal domain is responsible for binding to maltose, while the C-terminal domain is involved in signaling and regulation.

Function

MBP binds to maltose with high affinity, allowing bacteria to scavenge maltose from their environment for use as a carbon source. Upon binding maltose, MBP undergoes a conformational change that triggers downstream signaling pathways, leading to the activation of maltose transport systems in the cell membrane.

Applications

Due to its high affinity for maltose and stability, MBP is widely used as a fusion tag in recombinant protein expression systems. By fusing the target protein to MBP, researchers can improve protein solubility, stability, and expression levels. Additionally, MBP can be used in affinity chromatography to purify maltose-binding proteins or proteins fused to MBP.

See also

• Periplasmic binding protein
• Recombinant protein expression
• Affinity chromatography

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