Arabinose-binding protein, bacterial

Amino acids involved in binding M6P are shown in O Fig. 8. The phosphate moiety is coordinated by His 105, Asn 104, Asp 103 and divalent cation. Each hydroxyl of Man is hydrogen-bonded to binding site residues, while no interactions between the hydrophobic carbohydrate backbone and aromatic side chains are observed [148]. The multiple contacts between lectin and M6P, in contrast to that observed for many lectins which mediate cell surface interactions, are reflected in pM binding constants, reminiscent of bacterial arabinose-binding protein which functions as a sugar transport protein [149]. 

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