Molecular analysis of cyclic α-maltosyl-(1â6)-maltose binding protein in the bacterial metabolic pathway.
PLoS One
; 15(11): e0241912, 2020.
Article
in En
| MEDLINE
| ID: mdl-33211750
ABSTRACT
Cyclic α-maltosyl-(1â6)-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-(1â6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arthrobacter
/
Maltose-Binding Proteins
Language:
En
Journal:
PLoS One
Journal subject:
CIENCIA
/
MEDICINA
Year:
2020
Document type:
Article
Affiliation country:
Japón