Neutron crystallographic studies reveal hydrogen bond and water-mediated interactions between a carbohydrate-binding module and its bound carbohydrate ligand.
Biochemistry
; 54(42): 6435-8, 2015 Oct 27.
Article
de En
| MEDLINE
| ID: mdl-26451738
ABSTRACT
Carbohydrate-binding modules (CBMs) are key components of many carbohydrate-modifying enzymes. CBMs affect the activity of these enzymes by modulating bonding and catalysis. To further characterize and study CBM-ligand binding interactions, neutron crystallographic studies of an engineered family 4-type CBM in complex with a branched xyloglucan ligand were conducted. The first neutron crystal structure of a CBM-ligand complex reported here shows numerous atomic details of hydrogen bonding and water-mediated interactions and reveals the charged state of key binding cleft amino acid side chains.
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Glucides
/
Endo-1,4-beta xylanases
/
Métabolisme glucidique
Langue:
En
Journal:
Biochemistry
Année:
2015
Type de document:
Article
Pays d'affiliation:
Suède