Molecular analysis of cyclic α-maltosyl-(1â6)-maltose binding protein in the bacterial metabolic pathway.
PLoS One
; 15(11): e0241912, 2020.
Article
em 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.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Arthrobacter
/
Proteínas Ligantes de Maltose
Idioma:
En
Revista:
PLoS One
Assunto da revista:
CIENCIA
/
MEDICINA
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Japão