Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of β-1,3-glucan.

ABSTRACT: BH0236 from Bacillus halodurans is a multimodular β-1,3-glucanase comprising an N-terminal family 81 glycoside hydrolase catalytic module, an internal family 6 carbohydrate-binding module (CBM) that binds the nonreducing end of β-1,3-glucan chains, and an uncharacterized C-terminal module classified into CBM family 56. Here, we determined that this latter CBM, BhCBM56, bound the soluble β-1,3-glucan laminarin with a dissociation constant (K_d ) of ∼26 μm and displayed higher affinity for insoluble β-1,3-glucans with K_d values of ∼2-10 μm but lacked affinity for β-1,3-glucooligosaccharides. The X-ray crystal structure of BhCBM56 and NMR-derived chemical shift mapping of the binding site revealed a β-sandwich fold, with the face of one β-sheet posses

SUBMITTER: Hettle A 

PROVIDER: S-EPMC5641894 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature