Structural highlights
Function
D2YYD8_ARTGO
Publication Abstract from PubMed
Cyclic alpha-maltosyl-(1-->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 Kd value of 9.6 nM. The crystal structure of CMMBP was determined at a resolution of 1.47 A, 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-->6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.
Molecular analysis of cyclic alpha-maltosyl-(1-->6)-maltose binding protein in the bacterial metabolic pathway.,Kohno M, Arakawa T, Sunagawa N, Mori T, Igarashi K, Nishimoto T, Fushinobu S PLoS One. 2020 Nov 19;15(11):e0241912. doi: 10.1371/journal.pone.0241912. , eCollection 2020. PMID:33211750[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kohno M, Arakawa T, Sunagawa N, Mori T, Igarashi K, Nishimoto T, Fushinobu S. Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway. PLoS One. 2020 Nov 19;15(11):e0241912. PMID:33211750 doi:10.1371/journal.pone.0241912
