Molecular analysis of cyclic [alpha]-maltosyl

Cyclic [alpha]-maltosyl-(1[right arrow]6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating [alpha]-1,4 and [alpha]-1,6 linkages. Here, we report functional and structural analyses on CMM-binding protein (CMMBP), which is a substrate-binding protein (SBP) of an ABC importer system of the bacteria Arthrobacter globiformis. Isothermal titration calorimetry analysis revealed that CMMBP specifically bound to CMM with a K.sub.d value of 9.6 nM. The crystal structure of CMMBP was determined at a resolution of 1.47 Å, and a panose molecule was bound in a cleft between two domains. To delineate its structural features, the crystal structure of CMMBP was compared with other SBPs specific for carbohydrates, such as cyclic [alpha]-nigerosyl-(1[right arrow]6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.