Structural insights into curdlan degradation via a glycoside hydrolase containing a disruptive carbohydrate-binding module.

ABSTRACT:

Background

Degradation via enzymatic processes for the production of valuable β-1,3-glucooligosaccharides (GOS) from curdlan has attracted considerable interest. CBM6E functions as a curdlan-specific β-1,3-endoglucanase, composed of a glycoside hydrolase family 128 (GH128) module and a carbohydrate-binding module (CBM) derived from family CBM6.

Results

Crystallographic analyses were conducted to comprehend the substrate specificity mechanism of CBM6E. This unveiled structures of both apo CBM6E and its GOS-complexed form. The GH128 and CBM6 modules constitute a cohesive unit, binding nine glucoside moieties within the catalytic groove in a singular helical conformation. By extending the substrate-binding groove, we engineered CBM6E variants with heightened hydrolytic activiti

SUBMITTER: Lv T 

PROVIDER: S-EPMC10956234 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature