N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH.

ABSTRACT: Many carbohydrate-active enzymes have complex architectures comprising multiple modules that may be involved in catalysis, carbohydrate binding, or protein-protein interactions. Carbohydrate-binding modules (CBMs) are a common ancillary module whose function is to promote the adherence of the complete enzyme to carbohydrate substrates. CBM family 32 has been proposed to be one of the most diverse CBM families classified to date, yet all of the structurally characterized CBM32s thus far recognize galactose-based ligands. Here, we report a unique binding specificity and mode of ligand binding for a family 32 CBM. NagHCBM32-2 is one of four CBM32 modules in NagH, a family 84 glycoside hydrolase secreted by Clostridium perfringens. NagHCBM32-2 has the beta-sandwich scaffold common to members o

SUBMITTER: Ficko-Blean E 

PROVIDER: S-EPMC2937040 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature