Crystal Structure of Bifidobacterium bifidum Glycoside Hydrolase Family 110 α-Galactosidase Specific for Blood Group B Antigen.

ABSTRACT: To overcome incompatibility issues and increase the possibility of blood transfusion, technologies that enable efficient conversion of A- and B-type red blood cells to the universal donor O-type is desirable. Although several blood type-converting enzymes have been identified, detailed understanding about their molecular functions is limited. α-Galactosidase from Bifidobacterium bifidum JCM 1254 (AgaBb), belonging to glycoside hydrolase (GH) 110 subfamily A, specifically acts on blood group B antigen. Here we present the crystal structure of AgaBb, including the catalytic GH110 domain and part of the C-terminal uncharacterized regions. Based on this structure, we deduced a possible binding mechanism of blood group B antigen to the active site. Site-directed mutagenesis confirmed tha

SUBMITTER: Kashima T 

PROVIDER: S-EPMC11368712 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature