Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway

Masaki Kohno, Takatoshi Arakawa, Naoki Sunagawa, Tetsuya Mori, Kiyohiko Igarashi, Tomoyuki Nishimoto, Shinya Fushinobu (Corresponding Author)

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Abstract

Cyclic α-maltosyl-(1→6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating α-1,4 and α-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 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 α-nigerosyl-(1→6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.

Original languageEnglish
Article numbere0241912
Pages (from-to)e0241912
JournalPLoS ONE
Volume15
Issue number11
DOIs
Publication statusPublished - Nov 2020
MoE publication typeA1 Journal article-refereed

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